Crystal structure of HLA-G presenting KLPAQFYIL peptide. Determined by X-ray diffraction at 1.7 Å resolution. Released 23 Feb 2010.
Explore 3KYO in 3D Show helices and sheets RCSB PDB PDBe
3KYO contains 29 α-helices and 60 β-strands across 4 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 | 111-118 | 8 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-194 | 9 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-224 | 3 | 4 |
| β-strand | 229-230 | 2 | 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 |
|---|---|---|---|
| β-strand | 4-12 | 9 | 8 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 109-118 | 10 | 8 |
| β-strand | 121-126 | 6 | 8 |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 9 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-194 | 9 | 10 |
| β-strand | 198-208 | 11 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 214-219 | 6 | 11 |
| β-strand | 222-223 | 2 | 11 |
| α-helix | 224 | 1 | |
| β-strand | 228-230 | 3 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-250 | 10 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 270-272 | 3 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I antigen | A, C | protein | 273 | Homo sapiens | P17693 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| KLPAQFYIL peptide | P, Q | protein | 9 |
>3KYO_1 MHC class I antigen (chains A, C) SHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSASPRMEPRAPWVEQEGPEYWE EETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLIRGYERYAYDGK DYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQR ADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTF QKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRW
>3KYO_2 Beta-2-microglobulin (chains B, D) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>3KYO_3 KLPAQFYIL peptide (chains P, Q) KLPAQFYIL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CO | Cobalt (II) ion | Co | 2 |
The structure and stability of the monomorphic HLA-G are influenced by the nature of the bound peptide. Walpole, N.G., Kjer-Nielsen, L., Kostenko, L. et al. J Mol Biol (2010) 397:467-480. DOI 10.1016/j.jmb.2010.01.052 · PubMed
Other PDB entries of the same protein (UniProt P17693 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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