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415  structures 7359  species 0  interactions 44941  sequences 390  architectures

Family: Fer2 (PF00111)

Summary: 2Fe-2S iron-sulfur cluster binding domain

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 "Ferredoxin". More...

Ferredoxin Edit Wikipedia article

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.[1][2]

Another redox protein, isolated from spinach chloroplasts, was termed "chloroplast ferredoxin".[3] The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight-excited chlorophyll and transfers them to the enzyme ferredoxin: NADP+ oxidoreductase EC 1.18.1.2.

Ferredoxins are small proteins containing iron and sulfur atoms organized as iron–sulfur clusters. These biological "capacitors" can accept or discharge electrons, with the effect of a change in the oxidation state of the iron atoms between +2 and +3. In this way, ferredoxin acts as an electron transfer agent in biological redox reactions.

Other bioinorganic electron transport systems include rubredoxins, cytochromes, blue copper proteins, and the structurally related Rieske proteins.

Ferredoxins can be classified according to the nature of their iron–sulfur clusters and by sequence similarity.

Fe2S2 ferredoxins

2Fe-2S iron-sulfur cluster binding domain
Fe2S2.svg
Structural representation of an Fe2S2 ferredoxin.
Identifiers
SymbolFer2
PfamPF00111
Pfam clanCL0486
InterProIPR001041
PROSITEPDOC00642
SCOPe3fxc / SUPFAM
OPM protein1kf6

Members of the 2Fe–2S ferredoxin superfamily (InterProIPR036010) have a general core structure consisting of beta(2)-alpha-beta(2), which includes putidaredoxin, terpredoxin, and adrenodoxin.[4][5][6][7] They are proteins of around one hundred amino acids with four conserved cysteine residues to which the 2Fe–2S cluster is ligated. This conserved region is also found as a domain in various metabolic enzymes and in multidomain proteins, such as aldehyde oxidoreductase (N-terminal), xanthine oxidase (N-terminal), phthalate dioxygenase reductase (C-terminal), succinate dehydrogenase iron–sulphur protein (N-terminal), and methane monooxygenase reductase (N-terminal).

Plant-type ferredoxins

One group of ferredoxins, originally found in chloroplast membranes, has been termed "chloroplast-type" or "plant-type" (InterProIPR010241). Its active center is a [Fe2S2] cluster, where the iron atoms are tetrahedrally coordinated both by inorganic sulfur atoms and by sulfurs of four conserved cysteine (Cys) residues.

In chloroplasts, Fe2S2 ferredoxins function as electron carriers in the photosynthetic electron transport chain and as electron donors to various cellular proteins, such as glutamate synthase, nitrite reductase and sulfite reductase. In hydroxylating bacterial dioxygenase systems, they serve as intermediate electron-transfer carriers between reductase flavoproteins and oxygenase.

Thioredoxin-like ferredoxins

The Fe2S2 ferredoxin from Clostridium pasteurianum (Cp2FeFd; P07324) has been recognized as distinct protein family on the basis of its amino acid sequence, spectroscopic properties of its iron–sulfur cluster and the unique ligand swapping ability of two cysteine ligands to the [Fe2S2] cluster. Although the physiological role of this ferredoxin remains unclear, a strong and specific interaction of Cp2FeFd with the molybdenum-iron protein of nitrogenase has been revealed. Homologous ferredoxins from Azotobacter vinelandii (Av2FeFdI; P82802) and Aquifex aeolicus (AaFd; O66511) have been characterized. The crystal structure of AaFd has been solved. AaFd exists as a dimer. The structure of AaFd monomer is different from other Fe2S2 ferredoxins. The fold belongs to the α+β class, with first four β-strands and two α-helices adopting a variant of the thioredoxin fold.[8] UniProt categorizes these as the "2Fe2S Shethna-type ferredoxin" family.[9]

Adrenodoxin-type ferredoxins

ferredoxin 1
3P1M.pdb1.png
Crystal structure of human ferredoxin-1 (FDX1).[10]
Identifiers
SymbolFDX1
Alt. symbolsFDX
NCBI gene2230
HGNC3638
OMIM103260
RefSeqNM_004109
UniProtP10109
Other data
LocusChr. 11 q22.3

Adrenodoxin (adrenal ferredoxin; InterProIPR001055), putidaredoxin, and terpredoxin make up a family of soluble Fe2S2 proteins that act as single electron carriers, mainly found in eukaryotic mitochondria and Proteobacteria. The human variant of adrenodoxin is referred to as ferredoxin-1 and ferredoxin-2. In mitochondrial monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound cytochrome P450. In bacteria, putidaredoxin and terpredoxin transfer electrons between corresponding NADH-dependent ferredoxin reductases and soluble P450s.[11][12] The exact functions of other members of this family are not known, although Escherichia coli Fdx is shown to be involved in biogenesis of Fe–S clusters.[13] Despite low sequence similarity between adrenodoxin-type and plant-type ferredoxins, the two classes have a similar folding topology.

Ferredoxin-1 in humans participates in the synthesis of thyroid hormones. It also transfers electrons from adrenodoxin reductase to CYP11A1, a CYP450 enzyme responsible for cholesterol side chain cleavage. FDX-1 has the capability to bind to metals and proteins.[14] Ferredoxin-2 participates in heme A and iron–sulphur protein synthesis.[15]

Fe4S4 and Fe3S4 ferredoxins

The [Fe4S4] ferredoxins may be further subdivided into low-potential (bacterial-type) and high-potential (HiPIP) ferredoxins.

Low- and high-potential ferredoxins are related by the following redox scheme:

FdRedox.png

The formal oxidation numbers of the iron ions can be [2Fe3+, 2Fe2+] or [1Fe3+, 3Fe2+] in low-potential ferredoxins. The oxidation numbers of the iron ions in high-potential ferredoxins can be [3Fe3+, 1Fe2+] or [2Fe3+, 2Fe2+].

Bacterial-type ferredoxins

3Fe-4S binding domain
Fe3S4.png
Structural representation of an Fe3S4 ferredoxin.
Identifiers
SymbolFer4
PfamPF00037
InterProIPR001450
PROSITEPDOC00176
SCOPe5fd1 / SUPFAM
OPM protein1kqf

A group of Fe4S4 ferredoxins, originally found in bacteria, has been termed "bacterial-type". Bacterial-type ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including four cysteine residues that bind to a [Fe4S4] cluster. In Pyrococcus furiosus Fe4S4 ferredoxin, one of the conserved Cys residues is substituted with aspartic acid.

During the evolution of bacterial-type ferredoxins, intrasequence gene duplication, transposition and fusion events occurred, resulting in the appearance of proteins with multiple iron–sulfur centers. In some bacterial ferredoxins, one of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron–sulfur binding property or bind to a [Fe3S4] cluster instead of a [Fe4S4] cluster[16] and dicluster-type.[17]

3-D structures are known for a number of monocluster and dicluster bacterial-type ferredoxins. The fold belongs to the α+β class, with 2-7 α-helices and four β-strands forming a barrel-like structure, and an extruded loop containing three "proximal" Cys ligands of the iron–sulfur cluster.

High-potential iron–sulfur proteins

High potential iron–sulfur proteins (HiPIPs) form a unique family of Fe4S4 ferredoxins that function in anaerobic electron transport chains. Some HiPIPs have a redox potential higher than any other known iron–sulfur protein (e.g., HiPIP from Rhodopila globiformis has a redox potential of ca. 450 mV). Several HiPIPs have so far been characterized structurally, their folds belonging to the α+β class. As in other bacterial ferredoxins, the [Fe4S4] unit forms a cubane-type cluster and is ligated to the protein via four Cys residues.

Human proteins from ferredoxin family

References

  1. ^ Mortenson LE, Valentine RC, Carnahan JE (June 1962). "An electron transport factor from Clostridium pasteurianum". Biochemical and Biophysical Research Communications. 7 (6): 448–52. doi:10.1016/0006-291X(62)90333-9. PMID 14476372.
  2. ^ Valentine RC (December 1964). "BACTERIAL FERREDOXIN". Bacteriological Reviews. 28: 497–517. PMC 441251. PMID 14244728.
  3. ^ Tagawa K, Arnon DI (August 1962). "Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas". Nature. 195 (4841): 537–43. Bibcode:1962Natur.195..537T. doi:10.1038/195537a0. PMID 14039612.
  4. ^ Armengaud J, Sainz G, Jouanneau Y, Sieker LC (February 2001). "Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus". Acta Crystallographica Section D. 57 (Pt 2): 301–3. doi:10.1107/S0907444900017832. PMID 11173487.
  5. ^ Sevrioukova IF (April 2005). "Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida". Journal of Molecular Biology. 347 (3): 607–21. doi:10.1016/j.jmb.2005.01.047. PMID 15755454.
  6. ^ Mo H, Pochapsky SS, Pochapsky TC (April 1999). "A model for the solution structure of oxidized terpredoxin, a Fe2S2 ferredoxin from Pseudomonas". Biochemistry. 38 (17): 5666–75. CiteSeerX 10.1.1.34.4745. doi:10.1021/bi983063r. PMID 10220356.
  7. ^ Beilke D, Weiss R, Löhr F, Pristovsek P, Hannemann F, Bernhardt R, Rüterjans H (June 2002). "A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin". Biochemistry. 41 (25): 7969–78. doi:10.1021/bi0160361. PMID 12069587.
  8. ^ Yeh AP, Ambroggio XI, Andrade SL, Einsle O, Chatelet C, Meyer J, Rees DC (September 2002). "High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus". The Journal of Biological Chemistry. 277 (37): 34499–507. doi:10.1074/jbc.M205096200. PMID 12089152.
  9. ^ family:"2fe2s shethna type ferredoxin family"
  10. ^ PDB: 3P1M​; Chaikuad A, Johansson, C, Krojer, T, Yue, WW, Phillips, C, Bray, JE, Pike, ACW, Muniz, JRC, Vollmar, M, Weigelt, J, Arrowsmith, CH, Edwards, AM, Bountra, C, Kavanagh, K, Oppermann, U (2010). "Crystal structure of human ferredoxin-1 (FDX1) in complex with iron-sulfur cluster". To be Published. doi:10.2210/pdb3p1m/pdb.
  11. ^ Peterson JA, Lorence MC, Amarneh B (April 1990). "Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins". The Journal of Biological Chemistry. 265 (11): 6066–73. PMID 2180940.
  12. ^ Peterson JA, Lu JY, Geisselsoder J, Graham-Lorence S, Carmona C, Witney F, Lorence MC (July 1992). "Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon". The Journal of Biological Chemistry. 267 (20): 14193–203. PMID 1629218.
  13. ^ Tokumoto U, Takahashi Y (July 2001). "Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins". Journal of Biochemistry. 130 (1): 63–71. doi:10.1093/oxfordjournals.jbchem.a002963. PMID 11432781.
  14. ^ "Entrez Gene: FDX1 ferredoxin 1".
  15. ^ "FDX2 ferredoxin 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 8 April 2019.
  16. ^ Fukuyama K, Matsubara H, Tsukihara T, Katsube Y (November 1989). "Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins". Journal of Molecular Biology. 210 (2): 383–98. doi:10.1016/0022-2836(89)90338-0. PMID 2600971.
  17. ^ Duée ED, Fanchon E, Vicat J, Sieker LC, Meyer J, Moulis JM (November 1994). "Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution". Journal of Molecular Biology. 243 (4): 683–95. doi:10.1016/0022-2836(94)90041-8. PMID 7966291.

Further reading

External links

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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.

2Fe-2S iron-sulfur cluster binding domain Provide feedback

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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001041

Ferredoxins are small, acidic, electron transfer proteins that are ubiquitous in biological redox systems. They have either 4Fe-4S, 3Fe-4S, or 2Fe-2S cluster. Among them, ferredoxin with one 2Fe-2S cluster per molecule are present in plants, animals, and bacteria, and form a distinct Ferredoxin family [ PUBMED:2065785 ]. They are proteins of around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This conserved region is also found as a domain in various metabolic enzymes.

Several structures of the 2Fe-2S ferredoxin-type domain have been determined [ PUBMED:8586613 ]. The domain is classified as a beta-grasp, which is characterised as having a beta-sheet comprised of four beta-strands and one alpha-helix flanking the sheet. The two Fe atoms are coordinated tetrahedrally by the two inorganic S atoms and four cysteinyl S atoms.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 Fer2 (CL0486), which has the following description:

The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domani is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.

The clan contains the following 5 members:

DHODB_Fe-S_bind Fer2 Fer2_2 Fer2_3 Fer2_4

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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  Seed
(206)
Full
(44941)
Representative proteomes UniProt
(194642)
RP15
(5016)
RP35
(19441)
RP55
(44601)
RP75
(80830)
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  Seed
(206)
Full
(44941)
Representative proteomes UniProt
(194642)
RP15
(5016)
RP35
(19441)
RP55
(44601)
RP75
(80830)
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  Seed
(206)
Full
(44941)
Representative proteomes UniProt
(194642)
RP15
(5016)
RP35
(19441)
RP55
(44601)
RP75
(80830)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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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.

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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: Prosite
Previous IDs: fer2;
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL
Number in seed: 206
Number in full: 44941
Average length of the domain: 75.20 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 22.39 %

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 20.9 15.0
Trusted cut-off 20.9 15.0
Noise cut-off 20.8 14.9
Model length: 78
Family (HMM) version: 29
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence

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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 Fer2 domain has been found. There are 415 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
A0A0P0X4G4 View 3D Structure Click here
A0A0R0G5H5 View 3D Structure Click here
A0A0R0GLS0 View 3D Structure Click here
A0A0R0JTR0 View 3D Structure Click here
A0A1D6EVV4 View 3D Structure Click here
A0A1D6FPD0 View 3D Structure Click here
A0A1D6GFT6 View 3D Structure Click here
A0A1D6HX68 View 3D Structure Click here
A0A1D6JN19 View 3D Structure Click here
A0A1D6K6B9 View 3D Structure Click here
A0A1D6L715 View 3D Structure Click here
A0A1D6L725 View 3D Structure Click here
A0A1D6L755 View 3D Structure Click here
A0A1D6M542 View 3D Structure Click here
A0A1D6MBZ6 View 3D Structure Click here
A0A1D6MF08 View 3D Structure Click here
A0A1D6NT01 View 3D Structure Click here
A0A1D6PRE2 View 3D Structure Click here
A0A1D8PJS2 View 3D Structure Click here
A0A2R8Q1T4 View 3D Structure Click here
A0A2R8QF75 View 3D Structure Click here
A0A368UHS1 View 3D Structure Click here
A4I234 View 3D Structure Click here
A4I755 View 3D Structure Click here
A4I756 View 3D Structure Click here
A4I757 View 3D Structure Click here
A4I758 View 3D Structure Click here
B1P758 View 3D Structure Click here
B1P759 View 3D Structure Click here
B4F9V1 View 3D Structure Click here
B4FVP6 View 3D Structure Click here
B4FYW4 View 3D Structure Click here
B6SP61 View 3D Structure Click here
B6U5I8 View 3D Structure Click here
C0P8C8 View 3D Structure Click here
C0PJD4 View 3D Structure Click here
C6SVS3 View 3D Structure Click here
C6SX14 View 3D Structure Click here
C6SX81 View 3D Structure Click here
C6T195 View 3D Structure Click here
C6T1B0 View 3D Structure Click here
C6T1J0 View 3D Structure Click here
C6T265 View 3D Structure Click here
C6TNZ4 View 3D Structure Click here
D4A8N2 View 3D Structure Click here
E7F7J1 View 3D Structure Click here
F1Q5R8 View 3D Structure Click here
F4JLI5 View 3D Structure Click here
F4JUE0 View 3D Structure Click here
G3X982 View 3D Structure Click here
I1JIN7 View 3D Structure Click here
I1K498 View 3D Structure Click here
I1LTF4 View 3D Structure Click here
I1LY98 View 3D Structure Click here
I1M510 View 3D Structure Click here
I1M7D9 View 3D Structure Click here
I1MCT0 View 3D Structure Click here
I1MS45 View 3D Structure Click here
I1MVE7 View 3D Structure Click here
I1MWM4 View 3D Structure Click here
K7KB27 View 3D Structure Click here
K7L5E5 View 3D Structure Click here
K7LMC9 View 3D Structure Click here
K7LVE8 View 3D Structure Click here
M1ZMM0 View 3D Structure Click here
O04090 View 3D Structure Click here
O17892 View 3D Structure Click here
O23344 View 3D Structure Click here
O23887 View 3D Structure Click here
O23888 View 3D Structure Click here
O53669 View 3D Structure Click here
O53709 View 3D Structure Click here
O54754 View 3D Structure Click here
O61198 View 3D Structure Click here
O80429 View 3D Structure Click here
O86347 View 3D Structure Click here
P0A9R4 View 3D Structure Click here
P0ABW3 View 3D Structure Click here
P10109 View 3D Structure Click here
P10351 View 3D Structure Click here
P16972 View 3D Structure Click here
P22985 View 3D Structure Click here
P24483 View 3D Structure Click here
P27787 View 3D Structure Click here
P27788 View 3D Structure Click here
P27789 View 3D Structure Click here
P37193 View 3D Structure Click here
P46656 View 3D Structure Click here
P47989 View 3D Structure Click here
P71846 View 3D Structure Click here
P75824 View 3D Structure Click here
P75863 View 3D Structure Click here
P76081 View 3D Structure Click here
P76254 View 3D Structure Click here
P77165 View 3D Structure Click here
P94044 View 3D Structure Click here
P95277 View 3D Structure Click here
P9WIV9 View 3D Structure Click here
P9WJ93 View 3D Structure Click here
P9WNE9 View 3D Structure Click here
Q00519 View 3D Structure Click here
Q06278 View 3D Structure Click here
Q08C57 View 3D Structure Click here
Q0J8M2 View 3D Structure Click here
Q10361 View 3D Structure Click here
Q10F16 View 3D Structure Click here
Q12184 View 3D Structure Click here
Q34312 View 3D Structure Click here
Q3TYQ9 View 3D Structure Click here
Q40684 View 3D Structure Click here
Q46801 View 3D Structure Click here
Q4CKU4 View 3D Structure Click here
Q4CT33 View 3D Structure Click here
Q4DDW9 View 3D Structure Click here
Q4DXE9 View 3D Structure Click here
Q54FB7 View 3D Structure Click here
Q55GW1 View 3D Structure Click here
Q57557 View 3D Structure Click here
Q5N7C3 View 3D Structure Click here
Q5QE78 View 3D Structure Click here
Q5QE79 View 3D Structure Click here
Q5QE80 View 3D Structure Click here
Q5SGK3 View 3D Structure Click here
Q69LJ8 View 3D Structure Click here
Q69R21 View 3D Structure Click here
Q6AUV1 View 3D Structure Click here
Q6I620 View 3D Structure Click here
Q6JAD2 View 3D Structure Click here
Q6P4F2 View 3D Structure Click here
Q75LK5 View 3D Structure Click here
Q7G191 View 3D Structure Click here
Q7G192 View 3D Structure Click here
Q7G193 View 3D Structure Click here
Q7G9P4 View 3D Structure Click here
Q7XH05 View 3D Structure Click here
Q7XHS1 View 3D Structure Click here
Q7XIU2 View 3D Structure Click here
Q7XVG7 View 3D Structure Click here
Q850T5 View 3D Structure Click here
Q852M1 View 3D Structure Click here
Q852M2 View 3D Structure Click here
Q8GUQ8 View 3D Structure Click here
Q8I5R0 View 3D Structure Click here
Q8IED5 View 3D Structure Click here
Q8IND5 View 3D Structure Click here
Q8S904 View 3D Structure Click here
Q8SZA8 View 3D Structure Click here
Q960A1 View 3D Structure Click here
Q9C7Y4 View 3D Structure Click here
Q9CPW2 View 3D Structure Click here
Q9FIA7 View 3D Structure Click here
Q9LU21 View 3D Structure Click here
Q9M0V0 View 3D Structure Click here
Q9NA32 View 3D Structure Click here
Q9VF53 View 3D Structure Click here
Q9Z0U5 View 3D Structure Click here
Q9ZQG8 View 3D Structure Click here