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620  structures 5745  species 0  interactions 33585  sequences 504  architectures

Family: Ion_trans_2 (PF07885)

Summary: Ion channel

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Ion channel family". More...

Ion channel family Edit Wikipedia article

  • From a page move: This is a redirect from a page that has been moved (renamed). This page was kept as a redirect to avoid breaking links, both internal and external, that may have been made to the old page name.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Voltage-gated potassium channel". More...

Voltage-gated potassium channel Edit Wikipedia article

Eukaryotic potassium channel
2r9r opm.png
Potassium channel, structure in a membrane-like environment. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
Identifiers
SymbolIon_trans
PfamPF00520
InterProIPR005821
SCOPe1bl8 / SUPFAM
TCDB1.A.1
OPM superfamily8
OPM protein2a79
Membranome217
Ion channel (bacterial)
1r3j.png
Potassium channel KcsA. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
Identifiers
SymbolIon_trans_2
PfamPF07885
InterProIPR013099
SCOPe1bl8 / SUPFAM
OPM protein1r3j
Slow voltage-gated potassium channel (Potassium channel, voltage-dependent, beta subunit, KCNE)
Identifiers
SymbolISK_Channel
PfamPF02060
InterProIPR000369
TCDB8.A.10
Membranome218
KCNQ voltage-gated potassium channe
Identifiers
SymbolKCNQ_channel
PfamPF03520
InterProIPR013821
Kv2 voltage-gated K+ channel
Identifiers
SymbolKv2channel
PfamPF03521
InterProIPR003973

Voltage-gated potassium channels (VGKCs) are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential. During action potentials, they play a crucial role in returning the depolarized cell to a resting state.

Classification

Alpha subunits

Alpha subunits form the actual conductance pore. Based on sequence homology of the hydrophobic transmembrane cores, the alpha subunits of voltage-gated potassium channels are grouped into 12 classes. These are labeled Kvα1-12.[1] The following is a list of the 40 known human voltage-gated potassium channel alpha subunits grouped first according to function and then subgrouped according to the Kv sequence homology classification scheme:

Delayed rectifier

slowly inactivating or non-inactivating

A-type potassium channel

rapidly inactivating

  • Kvα1.x - Shaker-related: Kv1.4 (KCNA4)
  • Kvα3.x - Shaw-related: Kv3.3 (KCNC3), Kv3.4 (KCNC4)
  • Kvα4.x - Shal-related: Kv4.1 (KCND1), Kv4.2 (KCND2), Kv4.3 (KCND3)

Outward-rectifying

  • Kvα10.x: Kv10.2 (KCNH5)

Inwardly-rectifying

Passes current more easily in the inward direction (into the cell, from outside).

Slowly activating

Modifier/silencer

Unable to form functional channels as homotetramers but instead heterotetramerize with Kvα2 family members to form conductive channels.

Beta subunits

Beta subunits are auxiliary proteins that associate with alpha subunits, sometimes in a α4β4 stoichiometry.[2] These subunits do not conduct current on their own but rather modulate the activity of Kv channels.[3]

Proteins minK and MiRP1 are putative hERG beta subunits.[6]

Animal research

The voltage-gated K+ channels that provide the outward currents of action potentials have similarities to bacterial K+ channels.

These channels have been studied by X-ray diffraction, allowing determination of structural features at atomic resolution.

The function of these channels is explored by electrophysiological studies.

Genetic approaches include screening for behavioral changes in animals with mutations in K+ channel genes. Such genetic methods allowed the genetic identification of the "Shaker" K+ channel gene in Drosophila before ion channel gene sequences were well known.

Study of the altered properties of voltage-gated K+ channel proteins produced by mutated genes has helped reveal the functional roles of K+ channel protein domains and even individual amino acids within their structures.

Structure

Typically, vertebrate voltage-gated K+ channels are tetramers of four identical subunits arranged as a ring, each contributing to the wall of the trans-membrane K+ pore. Each subunit is composed of six membrane spanning hydrophobic α-helical sequences, as well as a voltage sensor in S4. The intracellular side of the membrane contains both amino and carboxy termini.[7] The high resolution crystallographic structure of the rat Kvα1.2/β2 channel has recently been solved (Protein Databank Accession Number 2A79​),[8] and then refined in a lipid membrane-like environment (PDB: 2r9r​).

Selectivity

Voltage-gated K+ channels are selective for K+ over other cations such as Na+. There is a selectivity filter at the narrowest part of the transmembrane pore.

Channel mutation studies have revealed the parts of the subunits that are essential for ion selectivity. They include the amino acid sequence (Thr-Val-Gly-Tyr-Gly) or (Thr-Val-Gly-Phe-Gly) typical to the selectivity filter of voltage-gated K+ channels. As K+ passes through the pore, interactions between potassium ions and water molecules are prevented and the K+ interacts with specific atomic components of the Thr-Val-Gly-[YF]-Gly sequences from the four channel subunits [1].

It may seem counterintuitive that a channel should allow potassium ions but not the smaller sodium ions through. However in an aqueous environment, potassium and sodium cations are solvated by water molecules. When moving through the selectivity filter of the potassium channel, the water-K+ interactions are replaced by interactions between K+ and carbonyl groups of the channel protein. The diameter of the selectivity filter is ideal for the potassium cation, but too big for the smaller sodium cation. Hence the potassium cations are well "solvated" by the protein carbonyl groups, but these same carbonyl groups are too far apart to adequately solvate the sodium cation. Hence, the passage of potassium cations through this selectivity filter is strongly favored over sodium cations.

Open and closed conformations

The structure of the mammalian voltage-gated K+ channel has been used to explain its ability to respond to the voltage across the membrane. Upon opening of the channel, conformational changes in the voltage-sensor domains (VSD) result in the transfer of 12-13 elementary charges across the membrane electric field. This charge transfer is measured as a transient capacitive current that precedes opening of the channel. Several charged residues of the VSD, in particular four arginine residues located regularly at every third position on the S4 segment, are known to move across the transmembrane field and contribute to the gating charge. The position of these arginines, known as gating arginines, are highly conserved in all voltage-gated potassium, sodium, or calcium channels. However, the extent of their movement and their displacement across the transmembrane potential has been subject to extensive debate.[9] Specific domains of the channel subunits have been identified that are responsible for voltage-sensing and converting between the open and closed conformations of the channel. There are at least two closed conformations. In the first, the channel can open if the membrane potential becomes more positive. This type of gating is mediated by a voltage-sensing domain that consists of the S4 alpha helix that contains 6–7 positive charges. Changes in membrane potential cause this alpha helix to move in the lipid bilayer. This movement in turn results in a conformational change in the adjacent S5–S6 helices that form the channel pore and cause this pore to open or close. In the second, "N-type" inactivation, voltage-gated K+ channels inactivate after opening, entering a distinctive, closed conformation. In this inactivated conformation, the channel cannot open, even if the transmembrane voltage is favorable. The amino terminal domain of the K+ channel or an auxiliary protein can mediate "N-type" inactivation. The mechanism of this type of inactivation has been described as a "ball and chain" model, where the N-terminus of the protein forms a ball that is tethered to the rest of the protein through a loop (the chain).[10] The tethered ball blocks the inner porehole, preventing ion movement through the channel.[11][12]

Pharmacology

For blockers and activators of voltage gated potassium channels see: potassium channel blocker and potassium channel opener.

See also

References

  1. ^ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X (December 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacological Reviews. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104.
  2. ^ Pongs O, Leicher T, Berger M, Roeper J, Bähring R, Wray D, Giese KP, Silva AJ, Storm JF (April 1999). "Functional and molecular aspects of voltage-gated K+ channel beta subunits". Annals of the New York Academy of Sciences. 868 (Apr 30): 344–55. doi:10.1111/j.1749-6632.1999.tb11296.x. PMID 10414304.
  3. ^ Li Y, Um SY, McDonald TV (June 2006). "Voltage-gated potassium channels: regulation by accessory subunits". The Neuroscientist. 12 (3): 199–210. doi:10.1177/1073858406287717. PMID 16684966.
  4. ^ Zhang M, Jiang M, Tseng GN (May 2001). "minK-related peptide 1 associates with Kv4.2 and modulates its gating function: potential role as beta subunit of cardiac transient outward channel?". Circulation Research. 88 (10): 1012–9. doi:10.1161/hh1001.090839. PMID 11375270.
  5. ^ McCrossan ZA, Abbott GW (November 2004). "The MinK-related peptides". Neuropharmacology. 47 (6): 787–821. doi:10.1016/j.neuropharm.2004.06.018. PMID 15527815.
  6. ^ Anantharam A, Abbott GW (2005). Does hERG coassemble with a beta subunit? Evidence for roles of MinK and MiRP1. Novartis Foundation Symposium. Novartis Foundation Symposia. 266. pp. 100–12, discussion 112–7, 155–8. doi:10.1002/047002142X.fmatter. ISBN 9780470021408. PMID 16050264.
  7. ^ Yellen G (September 2002). "The voltage-gated potassium channels and their relatives". Nature. 419 (6902): 35–42. doi:10.1038/nature00978. PMID 12214225.
  8. ^ Long SB, Campbell EB, Mackinnon R (August 2005). "Crystal structure of a mammalian voltage-dependent Shaker family K+ channel". Science. 309 (5736): 897–903. doi:10.1126/science.1116269. PMID 16002581.
  9. ^ Lee SY, Lee A, Chen J, MacKinnon R (October 2005). "Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane". Proceedings of the National Academy of Sciences of the United States of America. 102 (43): 15441–6. doi:10.1073/pnas.0507651102. PMC 1253646. PMID 16223877.
  10. ^ Antz C, Fakler B (August 1998). "Fast Inactivation of Voltage-Gated K(+) Channels: From Cartoon to Structure" (PDF). News in Physiological Sciences. 13 (4): 177–182. PMID 11390785.
  11. ^ Armstrong CM, Bezanilla F (April 1973). "Currents related to movement of the gating particles of the sodium channels". Nature. 242 (5398): 459–61. doi:10.1038/242459a0. PMID 4700900.
  12. ^ Murrell-Lagnado RD, Aldrich RW (December 1993). "Energetics of Shaker K channels block by inactivation peptides". The Journal of General Physiology. 102 (6): 977–1003. doi:10.1085/jgp.102.6.977. PMC 2229186. PMID 8133246.

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Ion channel Provide feedback

This family includes the two membrane helix type ion channels found in bacteria.

Literature references

  1. Choe S; , Nat Rev Neurosci 2002;3:115-121.: Potassium channel structures. PUBMED:11836519 EPMC:11836519


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013099

This domain is found in a variety of potassium channel proteins, including the two membrane helix type ion channels found in bacteria [ PUBMED:11836519 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Ion_channel (CL0030), which has the following description:

This superfamily contains a diverse range of ion channels that share a pair of transmembrane helices in common. This clan is classified as the VIC (Voltage-gated Ion Channel) superfamily in TCDB.

The clan contains the following 7 members:

Ion_trans Ion_trans_2 IRK KdpA Lig_chan PKD_channel TrkH

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(96)
Full
(33585)
Representative proteomes UniProt
(87654)
RP15
(7552)
RP35
(16176)
RP55
(30939)
RP75
(43390)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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  Seed
(96)
Full
(33585)
Representative proteomes UniProt
(87654)
RP15
(7552)
RP35
(16176)
RP55
(30939)
RP75
(43390)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(96)
Full
(33585)
Representative proteomes UniProt
(87654)
RP15
(7552)
RP35
(16176)
RP55
(30939)
RP75
(43390)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_55 (release 15.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 96
Number in full: 33585
Average length of the domain: 81.40 aa
Average identity of full alignment: 20 %
Average coverage of the sequence by the domain: 22.70 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.5 22.5
Trusted cut-off 22.5 22.5
Noise cut-off 22.4 22.4
Model length: 79
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ion_trans_2 domain has been found. There are 620 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0K3AXZ4 View 3D Structure Click here
A0A0K3AXZ4 View 3D Structure Click here
A0A0R0G7U3 View 3D Structure Click here
A0A0R0G7U3 View 3D Structure Click here
A0A0R0GFP1 View 3D Structure Click here
A0A0R0GFP1 View 3D Structure Click here
A0A0R4IAI5 View 3D Structure Click here
A0A0R4IC13 View 3D Structure Click here
A0A0R4IF04 View 3D Structure Click here
A0A0R4IF04 View 3D Structure Click here
A0A0R4INU5 View 3D Structure Click here
A0A0R4ISF0 View 3D Structure Click here
A0A0R4ISF0 View 3D Structure Click here
A0A140LFQ8 View 3D Structure Click here
A0A140LFQ8 View 3D Structure Click here
A0A1D6ENT0 View 3D Structure Click here
A0A1D6ENT0 View 3D Structure Click here
A0A1D6I1N6 View 3D Structure Click here
A0A1D6I1N6 View 3D Structure Click here
A0A1D6M4T0 View 3D Structure Click here
A0A1D6NEP2 View 3D Structure Click here
A0A1D6NEP2 View 3D Structure Click here
A0A1D8PL65 View 3D Structure Click here
A0A1D8PL65 View 3D Structure Click here
A0A286Y8D0 View 3D Structure Click here
A0A286Y8D0 View 3D Structure Click here
A0A2R8PYU3 View 3D Structure Click here
A0A2R8PYU3 View 3D Structure Click here
A0A2R8QB85 View 3D Structure Click here
A0A2R8QBX7 View 3D Structure Click here
A0A2R8QBX7 View 3D Structure Click here
A0A2R8QJP1 View 3D Structure Click here
A0A2R8QJP1 View 3D Structure Click here
A0A2R8QM68 View 3D Structure Click here
A0A2X0RDZ3 View 3D Structure Click here
A0A2X0RDZ3 View 3D Structure Click here
A1EHR5 View 3D Structure Click here
A1EHR5 View 3D Structure Click here
A3QJX1 View 3D Structure Click here
A3QJX1 View 3D Structure Click here
A4HRK4 View 3D Structure Click here
A4HRK5 View 3D Structure Click here
A4HVZ5 View 3D Structure Click here
A4HVZ6 View 3D Structure Click here
A4HYK1 View 3D Structure Click here
A5PLK0 View 3D Structure Click here
A5PLK0 View 3D Structure Click here
A8DY93 View 3D Structure Click here
A8KB76 View 3D Structure Click here
A8KB76 View 3D Structure Click here
B0M0M8 View 3D Structure Click here
B0M0M8 View 3D Structure Click here
B2RVL1 View 3D Structure Click here
B2RVL1 View 3D Structure Click here
B4FJW7 View 3D Structure Click here
B4FJW7 View 3D Structure Click here
B5BNY0 View 3D Structure Click here
B5BNY0 View 3D Structure Click here
B8A573 View 3D Structure Click here
B8A573 View 3D Structure Click here
C0Z3L1 View 3D Structure Click here
C0Z3L1 View 3D Structure Click here
C4J1B8 View 3D Structure Click here
C4J1B8 View 3D Structure Click here
D3Z649 View 3D Structure Click here
D3ZLR9 View 3D Structure Click here
D3ZLR9 View 3D Structure Click here
D4A806 View 3D Structure Click here
D4A806 View 3D Structure Click here
E7F9C5 View 3D Structure Click here
E7F9C5 View 3D Structure Click here
E7F9D1 View 3D Structure Click here
E7F9D1 View 3D Structure Click here
E7FAT2 View 3D Structure Click here
E9QDN2 View 3D Structure Click here
E9QDN2 View 3D Structure Click here
F1Q5K8 View 3D Structure Click here
F1Q5K8 View 3D Structure Click here
F1Q9L9 View 3D Structure Click here
F1Q9L9 View 3D Structure Click here
F1QAI2 View 3D Structure Click here
F1QAI2 View 3D Structure Click here
F1QFA3 View 3D Structure Click here
F1QFA3 View 3D Structure Click here
F5GUD1 View 3D Structure Click here
F5GUD1 View 3D Structure Click here
G3V8R8 View 3D Structure Click here
G3V8R8 View 3D Structure Click here
G3V8V5 View 3D Structure Click here
G3V8V5 View 3D Structure Click here
G5E845 View 3D Structure Click here
G5E845 View 3D Structure Click here
G5EBQ2 View 3D Structure Click here
G5EBQ2 View 3D Structure Click here
G5ECW6 View 3D Structure Click here
G5ECW6 View 3D Structure Click here
G5ED42 View 3D Structure Click here
G5ED42 View 3D Structure Click here
G5EEH1 View 3D Structure Click here
G5EEH1 View 3D Structure Click here
G5EFI1 View 3D Structure Click here
G5EG92 View 3D Structure Click here
G5EG92 View 3D Structure Click here
G5EGD4 View 3D Structure Click here
G5EGD4 View 3D Structure Click here
H2KZ66 View 3D Structure Click here
H2KZ66 View 3D Structure Click here
H2L2J8 View 3D Structure Click here
H2L2J8 View 3D Structure Click here
H9G2R4 View 3D Structure Click here
I1JJJ2 View 3D Structure Click here
I1JJJ2 View 3D Structure Click here
I1JQW7 View 3D Structure Click here
I1JQW7 View 3D Structure Click here
I1MQY9 View 3D Structure Click here
I1MQY9 View 3D Structure Click here
I1NBH8 View 3D Structure Click here
I1NBH8 View 3D Structure Click here
I2HAD3 View 3D Structure Click here
I2HAD3 View 3D Structure Click here
K7KBC7 View 3D Structure Click here
K7KBC7 View 3D Structure Click here
K7KPW5 View 3D Structure Click here
K7L5I6 View 3D Structure Click here
K7L5I6 View 3D Structure Click here
M0R8B9 View 3D Structure Click here
M0R8B9 View 3D Structure Click here
O00180 View 3D Structure Click here
O00180 View 3D Structure Click here
O08581 View 3D Structure Click here
O08581 View 3D Structure Click here
O14649 View 3D Structure Click here
O14649 View 3D Structure Click here
O15554 View 3D Structure Click here
O17185 View 3D Structure Click here
O17185 View 3D Structure Click here
O17697 View 3D Structure Click here
O35111 View 3D Structure Click here
O35111 View 3D Structure Click here
O44773 View 3D Structure Click here
O45422 View 3D Structure Click here
O45422 View 3D Structure Click here
O45891 View 3D Structure Click here
O45891 View 3D Structure Click here
O45894 View 3D Structure Click here
O45894 View 3D Structure Click here
O53346 View 3D Structure Click here
O54912 View 3D Structure Click here
O54912 View 3D Structure Click here
O76791 View 3D Structure Click here
O76791 View 3D Structure Click here
O88454 View 3D Structure Click here
O88454 View 3D Structure Click here
O89109 View 3D Structure Click here
O95069 View 3D Structure Click here
O95069 View 3D Structure Click here
O95279 View 3D Structure Click here
O95279 View 3D Structure Click here
P31069 View 3D Structure Click here
P34410 View 3D Structure Click here
P34410 View 3D Structure Click here
P40310 View 3D Structure Click here
P40310 View 3D Structure Click here
P57789 View 3D Structure Click here
P57789 View 3D Structure Click here
P58390 View 3D Structure Click here
P58391 View 3D Structure Click here
P70604 View 3D Structure Click here
P70605 View 3D Structure Click here
P70606 View 3D Structure Click here
P90863 View 3D Structure Click here
P90863 View 3D Structure Click here
P97438 View 3D Structure Click here
P97438 View 3D Structure Click here
Q11122 View 3D Structure Click here
Q18120 View 3D Structure Click here
Q18120 View 3D Structure Click here
Q19525 View 3D Structure Click here
Q19525 View 3D Structure Click here
Q19907 View 3D Structure Click here
Q19907 View 3D Structure Click here
Q21467 View 3D Structure Click here
Q21467 View 3D Structure Click here
Q21529 View 3D Structure Click here
Q21529 View 3D Structure Click here
Q22042 View 3D Structure Click here
Q22042 View 3D Structure Click here
Q22043 View 3D Structure Click here
Q22043 View 3D Structure Click here
Q22271 View 3D Structure Click here
Q22271 View 3D Structure Click here
Q22940 View 3D Structure Click here
Q22940 View 3D Structure Click here
Q23297 View 3D Structure Click here
Q23297 View 3D Structure Click here
Q23386 View 3D Structure Click here
Q23386 View 3D Structure Click here
Q23435 View 3D Structure Click here
Q23435 View 3D Structure Click here
Q2QYI3 View 3D Structure Click here
Q32LX0 View 3D Structure Click here
Q32LX0 View 3D Structure Click here
Q3LS21 View 3D Structure Click here
Q3LS21 View 3D Structure Click here
Q3TBV4 View 3D Structure Click here
Q3TBV4 View 3D Structure Click here
Q4DHX0 View 3D Structure Click here
Q4DHX1 View 3D Structure Click here
Q4DP52 View 3D Structure Click here
Q4DUL7 View 3D Structure Click here
Q4DUL8 View 3D Structure Click here
Q4E0F3 View 3D Structure Click here
Q4E159 View 3D Structure Click here
Q4E5R5 View 3D Structure Click here
Q54SN1 View 3D Structure Click here
Q55CU6 View 3D Structure Click here
Q57604 View 3D Structure Click here
Q58752 View 3D Structure Click here
Q5FC72 View 3D Structure Click here
Q5FC72 View 3D Structure Click here
Q5JUK3 View 3D Structure Click here
Q5RGB0 View 3D Structure Click here
Q5RGB0 View 3D Structure Click here
Q5TZ59 View 3D Structure Click here
Q5TZ59 View 3D Structure Click here
Q5VSE6 View 3D Structure Click here
Q5VSE6 View 3D Structure Click here
Q65XY3 View 3D Structure Click here
Q69TN4 View 3D Structure Click here
Q69TN4 View 3D Structure Click here
Q6BES3 View 3D Structure Click here
Q6BES3 View 3D Structure Click here
Q6EUT8 View 3D Structure Click here
Q6EUT8 View 3D Structure Click here
Q6Q1P3 View 3D Structure Click here
Q6Q1P3 View 3D Structure Click here
Q6UVM3 View 3D Structure Click here
Q6UVM4 View 3D Structure Click here
Q6VV64 View 3D Structure Click here
Q6VV64 View 3D Structure Click here
Q6ZPR4 View 3D Structure Click here
Q76M80 View 3D Structure Click here
Q76M80 View 3D Structure Click here
Q7JZM1 View 3D Structure Click here
Q7JZM1 View 3D Structure Click here
Q7KMM5 View 3D Structure Click here
Q7KMM5 View 3D Structure Click here
Q7KVW5 View 3D Structure Click here
Q7YWY7 View 3D Structure Click here
Q7YWY7 View 3D Structure Click here
Q7Z418 View 3D Structure Click here
Q7Z418 View 3D Structure Click here
Q850M0 View 3D Structure Click here
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