Crystal structure of HLA-B*2709 complexed with the double citrullinated vasoactive intestinal peptide type 1 receptor (VIPR) peptide (residues 400-408). Determined by X-ray diffraction at 1.95 Å resolution. Released 9 Jun 2009.
Explore 3HCV in 3D Show helices and sheets RCSB PDB PDBe
3HCV contains 17 α-helices and 30 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| α-helix | 182 | 1 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class I histocompatibility antigen, B-27 alpha chain | A | protein | 276 | Homo sapiens | P01889 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Double citrullinated vasoactive intestinal polypeptide receptor | C | protein | 9 | P32241 (AlphaFold model) |
>3HCV_1 HLA class I histocompatibility antigen, B-27 alpha chain (chains A) GSHSMRYFHTSVSRPGRGEPRFITVGYVDDTLFVRFDSDAASPREEPRAPWIEQEGPEYW DRETQICKAKAQTDREDLRTLLRYYNQSEAGSHTLQNMYGCDVGPDGRLLRGYHQHAYDG KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGECVEWLRRYLENGKETLQ RADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
>3HCV_2 Beta-2-microglobulin (chains B) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>3HCV_3 DOUBLE CITRULLINATED VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR (chains C) RRKWRRWHL
Citrullination-and mhc polymorphism-dependent conformational changes of a self peptide. Beltrami, A., Rossmann, M., Gabdulkhakov, A. et al. To be published.
Other PDB entries of the same protein (UniProt P01889 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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