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18  structures 1504  species 0  interactions 20161  sequences 932  architectures

Family: zf-C3HC4 (PF00097)

Summary: Zinc finger, C3HC4 type (RING finger)

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 "RING finger domain". More...

RING finger domain Edit Wikipedia article

Zinc finger, C3HC4 type (RING finger)
1chc animated.gif
Structure of the C3HC4 domain.[1] Zinc ions are black spheres, coordinated by cysteines residues (blue).
Identifiers
Symbolzf-C3HC4
PfamPF00097
InterProIPR001841
SMARTSM00184
PROSITEPDOC00449
SCOPe1chc / SUPFAM

In molecular biology, a RING (Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C3HC4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).[2][3][4][5] This protein domain contains from 40 to 60 amino acids. Many proteins containing a RING finger play a key role in the ubiquitination pathway.

Zinc fingers

Zinc finger (Znf) domains are relatively small protein motifs that bind one or more zinc atoms, and which usually contain multiple finger-like protrusions that make tandem contacts with their target molecule. They bind DNA, RNA, protein and/or lipid substrates.[6][7][8][9][10] Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing.[11] Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

Some Zn finger domains have diverged such that they still maintain their core structure, but have lost their ability to bind zinc, using other means such as salt bridges or binding to other metals to stabilise the finger-like folds.

Function

Many RING finger domains simultaneously bind ubiquitination enzymes and their substrates and hence function as ligases. Ubiquitination in turn targets the substrate protein for degradation.[12][13][14]

Structure

The RING finger domain has the consensus sequence C-X2-C-X[9-39]-C-X[1-3]-H-X[2-3]-C-X2-C-X[4-48]-C-X2-C.[2] where:

  • C is a conserved cysteine residue involved zinc coordination,
  • H is a conserved histidine involved in zinc coordination,
  • Zn is zinc atom, and
  • X is any amino acid residue.

The following is a schematic representation of the structure of the RING finger domain:[2]

                              x x x     x x x
                             x      x x      x
                            x       x x       x
                           x        x x        x
                          C        C   C        C
                         x  \    / x   x \    /  x
                         x    Zn   x   x   Zn    x
                          C /    \ H   C /    \ C
                          x         x x         x
                 x x x x x x         x         x x x x x x

Examples

Examples of human genes which encode proteins containing a RING finger domain include:

AMFR, BBAP, BFAR, BIRC2, BIRC3, BIRC7, BIRC8, BMI1, BRAP, BRCA1, CBL, CBLB, CBLC, CBLL1, CHFR, COMMD3, DTX1, DTX2, DTX3, DTX3L, DTX4, DZIP3, HCGV, HLTF, HOIL-1, IRF2BP2, LNX1, LNX2, LONRF1, LONRF2, LONRF3, MARCH1, MARCH10, MARCH2, MARCH3, MARCH4, MARCH5, MARCH6, MARCH7, MARCH8, MARCH9, MDM2, MEX3A, MEX3B, MEX3C, MEX3D, MGRN1, MIB1, MID1, MID2, MKRN1, MKRN2, MKRN3, MKRN4, MNAT1, MYLIP, NFX1, NFX2, PCGF1, PCGF2, PCGF3, PCGF4, PCGF5, PCGF6, PDZRN3, PDZRN4, PEX10, PHRF1, PJA1, PJA2, PML, PML-RAR, PXMP3, RAD18, RAG1, RAPSN, RBCK1, RBX1, RC3H1, RC3H2, RCHY1, RFP2, RFPL1, RFPL2, RFPL3, RFPL4B, RFWD2, RFWD3, RING1, RNF2, RNF4, RNF5, RNF6, RNF7, RNF8, RNF10, RNF11, RNF12, RNF13, RNF14, RNF19A, RNF20, RNF24, RNF25, RNF26, RNF32, RNF38, RNF39, RNF40, RNF41, RNF43, RNF44, RNF55, RNF71, RNF103, RNF111, RNF113A, RNF113B, RNF121, RNF122, RNF123, RNF125, RNF126, RNF128, RNF130, RNF133, RNF135, RNF138, RNF139, RNF141, RNF144A, RNF145, RNF146, RNF148, RNF149, RNF150, RNF151, RNF152, RNF157, RNF165, RNF166, RNF167, RNF168, RNF169, RNF170, RNF175, RNF180, RNF181, RNF182, RNF185, RNF207, RNF213, RNF215, RNFT1, SH3MD4, SH3RF1, SH3RF2, SYVN1, TIF1, TMEM118, TOPORS, TRAF2, TRAF3, TRAF4, TRAF5, TRAF6, TRAF7, TRAIP, TRIM2, TRIM3, TRIM4, TRIM5, TRIM6, TRIM7, TRIM8, TRIM9, TRIM10, TRIM11, TRIM13, TRIM15, TRIM17, TRIM21, TRIM22, TRIM23, TRIM24, TRIM25, TRIM26, TRIM27, TRIM28, TRIM31, TRIM32, TRIM33, TRIM34, TRIM35, TRIM36, TRIM38, TRIM39, TRIM40, TRIM41, TRIM42, TRIM43, TRIM45, TRIM46, TRIM47, TRIM48, TRIM49, TRIM50, TRIM52, TRIM54, TRIM55, TRIM56, TRIM58, TRIM59, TRIM60, TRIM61, TRIM62, TRIM63, TRIM65, TRIM67, TRIM68, TRIM69, TRIM71, TRIM72, TRIM73, TRIM74, TRIML1, TTC3, UHRF1, UHRF2, VPS11, VPS8, ZNF179, ZNF294, ZNF313, ZNF364, ZNF650, ZNFB7, ZNRF1, ZNRF2, ZNRF3, ZNRF4, and ZSWIM2.

References

  1. ^ Barlow PN, Luisi B, Milner A, Elliott M, Everett R (March 1994). "Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger". J. Mol. Biol. 237 (2): 201–11. doi:10.1006/jmbi.1994.1222. PMID 8126734.
  2. ^ a b c Borden KL, Freemont PS (1996). "The RING finger domain: a recent example of a sequence-structure family". Curr. Opin. Struct. Biol. 6 (3): 395–401. doi:10.1016/S0959-440X(96)80060-1. PMID 8804826.
  3. ^ Hanson IM, Poustka A, Trowsdale J (1991). "New genes in the class II region of the human major histocompatibility complex". Genomics. 10 (2): 417–24. doi:10.1016/0888-7543(91)90327-B. PMID 1906426.
  4. ^ Freemont PS, Hanson IM, Trowsdale J (1991). "A novel cysteine-rich sequence motif". Cell. 64 (3): 483–4. doi:10.1016/0092-8674(91)90229-R. PMID 1991318.
  5. ^ Lovering R, Hanson IM, Borden KL, Martin S, O'Reilly NJ, Evan GI, Rahman D, Pappin DJ, Trowsdale J, Freemont PS (1993). "Identification and preliminary characterization of a protein motif related to the zinc finger". Proc. Natl. Acad. Sci. U.S.A. 90 (6): 2112–6. doi:10.1073/pnas.90.6.2112. PMC 46035. PMID 7681583.
  6. ^ Klug A (1999). "Zinc finger peptides for the regulation of gene expression". J. Mol. Biol. 293 (2): 215–8. doi:10.1006/jmbi.1999.3007. PMID 10529348.
  7. ^ Hall TM (2005). "Multiple modes of RNA recognition by zinc finger proteins". Curr. Opin. Struct. Biol. 15 (3): 367–73. doi:10.1016/j.sbi.2005.04.004. PMID 15963892.
  8. ^ Brown RS (2005). "Zinc finger proteins: getting a grip on RNA". Curr. Opin. Struct. Biol. 15 (1): 94–8. doi:10.1016/j.sbi.2005.01.006. PMID 15718139.
  9. ^ Gamsjaeger R, Liew CK, Loughlin FE, Crossley M, Mackay JP (2007). "Sticky fingers: zinc-fingers as protein-recognition motifs". Trends Biochem. Sci. 32 (2): 63–70. doi:10.1016/j.tibs.2006.12.007. PMID 17210253.
  10. ^ Matthews JM, Sunde M (2002). "Zinc fingers--folds for many occasions". IUBMB Life. 54 (6): 351–5. doi:10.1080/15216540216035. PMID 12665246.
  11. ^ Laity JH, Lee BM, Wright PE (2001). "Zinc finger proteins: new insights into structural and functional diversity". Curr. Opin. Struct. Biol. 11 (1): 39–46. doi:10.1016/S0959-440X(00)00167-6. PMID 11179890.
  12. ^ Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11364–9. doi:10.1073/pnas.96.20.11364. PMC 18039. PMID 10500182.
  13. ^ Joazeiro CA, Weissman AM (2000). "RING finger proteins: mediators of ubiquitin ligase activity". Cell. 102 (5): 549–52. doi:10.1016/S0092-8674(00)00077-5. PMID 11007473.
  14. ^ Freemont PS (2000). "RING for destruction?". Curr. Biol. 10 (2): R84–7. doi:10.1016/S0960-9822(00)00287-6. PMID 10662664.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR001841

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.

Zinc finger, C3HC4 type (RING finger) Provide feedback

The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid [1]. Many proteins containing a RING finger play a key role in the ubiquitination pathway [2].

Literature references

  1. Borden KL, Freemont PS; , Curr Opin Struct Biol 1996;6:395-401.: The RING finger domain: a recent example of a sequence-structure family. PUBMED:8804826 EPMC:8804826

  2. Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM; , Proc Natl Acad Sci U S A 1999;96:11364-11369.: RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. PUBMED:10500182 EPMC:10500182


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018957

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [ PUBMED:10529348 , PUBMED:15963892 , PUBMED:15718139 , PUBMED:17210253 , PUBMED:12665246 ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [ PUBMED:11179890 ]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid [ PUBMED:8804826 ]. Many proteins containing a RING finger play a key role in the ubiquitination pathway [ PUBMED:10500182 ].

Gene Ontology

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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

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
(35)
Full
(20161)
Representative proteomes UniProt
(47212)
RP15
(3640)
RP35
(9029)
RP55
(16959)
RP75
(22660)
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(35)
Full
(20161)
Representative proteomes UniProt
(47212)
RP15
(3640)
RP35
(9029)
RP55
(16959)
RP75
(22660)
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  Seed
(35)
Full
(20161)
Representative proteomes UniProt
(47212)
RP15
(3640)
RP35
(9029)
RP55
(16959)
RP75
(22660)
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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: Swissprot_feature_table
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL , Vella Briffa B
Number in seed: 35
Number in full: 20161
Average length of the domain: 44.20 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 6.90 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 20.7
Trusted cut-off 21.0 20.7
Noise cut-off 20.9 20.6
Model length: 41
Family (HMM) version: 27
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 zf-C3HC4 domain has been found. There are 18 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
A0A0G2K048 View 3D Structure Click here
A0A0G2KRG9 View 3D Structure Click here
A0A0G2KTY5 View 3D Structure Click here
A0A0G2QC40 View 3D Structure Click here
A0A0H2UKU5 View 3D Structure Click here
A0A0P0V8K7 View 3D Structure Click here
A0A0P0WM13 View 3D Structure Click here
A0A0P0XM35 View 3D Structure Click here
A0A0P0XVD7 View 3D Structure Click here
A0A0R0ESI4 View 3D Structure Click here
A0A0R0FLJ5 View 3D Structure Click here
A0A0R0GEU3 View 3D Structure Click here
A0A0R0GY98 View 3D Structure Click here
A0A0R0GZU6 View 3D Structure Click here
A0A0R0IMJ3 View 3D Structure Click here
A0A0R0J296 View 3D Structure Click here
A0A0R0J562 View 3D Structure Click here
A0A0R0KQH6 View 3D Structure Click here
A0A0R4ICA2 View 3D Structure Click here
A0A0R4ICU1 View 3D Structure Click here
A0A0R4IDG6 View 3D Structure Click here
A0A0R4IM45 View 3D Structure Click here
A0A0R4IWB8 View 3D Structure Click here
A0A1D6E4U1 View 3D Structure Click here
A0A1D6E647 View 3D Structure Click here
A0A1D6FBR8 View 3D Structure Click here
A0A1D6FR70 View 3D Structure Click here
A0A1D6H959 View 3D Structure Click here
A0A1D6HEG5 View 3D Structure Click here
A0A1D6HTQ2 View 3D Structure Click here
A0A1D6ICP3 View 3D Structure Click here
A0A1D6JAU4 View 3D Structure Click here
A0A1D6KTS9 View 3D Structure Click here
A0A1D6KUA1 View 3D Structure Click here
A0A1D6L7W8 View 3D Structure Click here
A0A1D6M3A7 View 3D Structure Click here
A0A1D6MQ54 View 3D Structure Click here
A0A1D6NZP1 View 3D Structure Click here
A0A1D6Q2S9 View 3D Structure Click here
A0A1D6QF58 View 3D Structure Click here
A0A1D8PFW5 View 3D Structure Click here
A0A1D8PJI9 View 3D Structure Click here
A0A1P8AWF9 View 3D Structure Click here
A0A1Z1CK50 View 3D Structure Click here
A0A286YAJ9 View 3D Structure Click here
A0A2R8PVA3 View 3D Structure Click here
A0A2R8Q2A8 View 3D Structure Click here
A0A2R8Q624 View 3D Structure Click here
A0A2R8QGD3 View 3D Structure Click here
A0A2R8QPQ7 View 3D Structure Click here
A0A2R8RJ75 View 3D Structure Click here
A4HS49 View 3D Structure Click here
A4HT31 View 3D Structure Click here
A4HTT2 View 3D Structure Click here
A4I068 View 3D Structure Click here
A4I3K9 View 3D Structure Click here
A4I5R4 View 3D Structure Click here
A4IDG5 View 3D Structure Click here
A6NGJ6 View 3D Structure Click here
A6NI03 View 3D Structure Click here
A8WFJ8 View 3D Structure Click here
A9C4A6 View 3D Structure Click here
B1WC90 View 3D Structure Click here
B4F9X1 View 3D Structure Click here
B4FCL8 View 3D Structure Click here
B4FHW7 View 3D Structure Click here
B5DFH7 View 3D Structure Click here
B6VQ60 View 3D Structure Click here
B7YZK8 View 3D Structure Click here
C0P3C8 View 3D Structure Click here
D3ZLN6 View 3D Structure Click here
D3ZRI0 View 3D Structure Click here
D3ZTX1 View 3D Structure Click here
D3ZY41 View 3D Structure Click here
D3ZYQ9 View 3D Structure Click here
D4A306 View 3D Structure Click here
D4AAZ8 View 3D Structure Click here
E0X9N4 View 3D Structure Click here
E7EXH5 View 3D Structure Click here
E7EZF3 View 3D Structure Click here
E7F2U0 View 3D Structure Click here
E7F4V8 View 3D Structure Click here
E7F6B0 View 3D Structure Click here
E7FAP1 View 3D Structure Click here
E9AG88 View 3D Structure Click here
E9PWL0 View 3D Structure Click here
F0IWS6 View 3D Structure Click here
F1QI34 View 3D Structure Click here
F1QJY4 View 3D Structure Click here
F1QS63 View 3D Structure Click here
F1QUH4 View 3D Structure Click here
F1QXU6 View 3D Structure Click here
F1QYX5 View 3D Structure Click here
F1R3C5 View 3D Structure Click here
F1R8W7 View 3D Structure Click here
F1R926 View 3D Structure Click here
F4I7D2 View 3D Structure Click here
F4ITM2 View 3D Structure Click here
F4IW24 View 3D Structure Click here
F4IWG7 View 3D Structure Click here
F4KGU4 View 3D Structure Click here
F8W3P8 View 3D Structure Click here
G3UY57 View 3D Structure Click here
G3V658 View 3D Structure Click here
G3V6K9 View 3D Structure Click here
G5EGI6 View 3D Structure Click here
H2KYS7 View 3D Structure Click here
I1JH54 View 3D Structure Click here
I1JTE1 View 3D Structure Click here
I1K556 View 3D Structure Click here
I1K7U3 View 3D Structure Click here
I1KLJ3 View 3D Structure Click here
I1KTL8 View 3D Structure Click here
I1KV48 View 3D Structure Click here
I1L1V3 View 3D Structure Click here
I1LBD4 View 3D Structure Click here
I1LNN5 View 3D Structure Click here
I1LTQ7 View 3D Structure Click here
I1M0B1 View 3D Structure Click here
I1M247 View 3D Structure Click here
I1MJM5 View 3D Structure Click here
I1MJM7 View 3D Structure Click here
I1N7J7 View 3D Structure Click here
I1NIY0 View 3D Structure Click here
I1YAP6 View 3D Structure Click here
K7KRW1 View 3D Structure Click here
K7L4K0 View 3D Structure Click here
K7LVV9 View 3D Structure Click here
K7LW27 View 3D Structure Click here
K7M1N1 View 3D Structure Click here
K7MA23 View 3D Structure Click here
K7MA52 View 3D Structure Click here
K7MC82 View 3D Structure Click here
K7MFH8 View 3D Structure Click here
K7MXM8 View 3D Structure Click here
M0R436 View 3D Structure Click here
M0R7W8 View 3D Structure Click here
M0RA58 View 3D Structure Click here
O00463 View 3D Structure Click here
O01481 View 3D Structure Click here
O13033 View 3D Structure Click here
O14212 View 3D Structure Click here
O17719 View 3D Structure Click here
O42845 View 3D Structure Click here
O60177 View 3D Structure Click here
O62427 View 3D Structure Click here
O70418 View 3D Structure Click here
O75150 View 3D Structure Click here
O81849 View 3D Structure Click here
O94271 View 3D Structure Click here
P0CE10 View 3D Structure Click here
P10862 View 3D Structure Click here
P15533 View 3D Structure Click here
P15919 View 3D Structure Click here
P24392 View 3D Structure Click here
P25172 View 3D Structure Click here
P28328 View 3D Structure Click here
P31244 View 3D Structure Click here
P32849 View 3D Structure Click here
P34537 View 3D Structure Click here
P36113 View 3D Structure Click here
P38398 View 3D Structure Click here
P39429 View 3D Structure Click here
P40072 View 3D Structure Click here
P48754 View 3D Structure Click here
P55098 View 3D Structure Click here
P70191 View 3D Structure Click here
P79051 View 3D Structure Click here
P86448 View 3D Structure Click here
P86449 View 3D Structure Click here
Q03601 View 3D Structure Click here
Q03605 View 3D Structure Click here
Q06003 View 3D Structure Click here
Q06587 View 3D Structure Click here
Q09268 View 3D Structure Click here
Q0J1Q7 View 3D Structure Click here
Q0J9V7 View 3D Structure Click here
Q10C16 View 3D Structure Click here
Q11096 View 3D Structure Click here
Q12933 View 3D Structure Click here
Q13064 View 3D Structure Click here
Q13434 View 3D Structure Click here
Q1ECU9 View 3D Structure Click here
Q1L8B2 View 3D Structure Click here
Q1L9F9 View 3D Structure Click here
Q1MTQ0 View 3D Structure Click here
Q2QUC7 View 3D Structure Click here
Q3TL54 View 3D Structure Click here
Q3U319 View 3D Structure Click here
Q3UWA4 View 3D Structure Click here
Q3V3A7 View 3D Structure Click here
Q498M5 View 3D Structure Click here
Q4D1I0 View 3D Structure Click here
Q4DB31 View 3D Structure Click here
Q4DMK1 View 3D Structure Click here
Q4DP57 View 3D Structure Click here
Q4DRP0 View 3D Structure Click here
Q4DT67 View 3D Structure Click here
Q4DXI0 View 3D Structure Click here
Q4E413 View 3D Structure Click here
Q4KLN8 View 3D Structure Click here
Q505D9 View 3D Structure Click here
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