3KYO: HLA-G presenting KLPAQFYIL peptide

Crystal structure of HLA-G presenting KLPAQFYIL peptide. Determined by X-ray diffraction at 1.7 Å resolution. Released 23 Feb 2010.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
6
Atoms
7,283
Mol. weight
89.27 kDa
Ligands
CO
Released
23 Feb 2010

Explore 3KYO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 11 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand3-12101
α-helix201
β-strand21-2881
β-strand31-3771
β-strand46-4721
α-helix50-523
α-helix57-8428
β-strand94-103101
β-strand111-11881
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-1587
α-helix159-1646
α-helix165-17410
α-helix176-1794
β-strand18312
α-helix184-1852
β-strand186-19493
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22434
β-strand229-23023
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chains B and D: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
α-helix461
β-strand50-5126
α-helix52-543
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain C: 12 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand4-1298
α-helix201
β-strand21-2888
β-strand31-3778
β-strand46-4728
α-helix50-523
α-helix57-8428
β-strand94-103108
β-strand109-118108
β-strand121-12668
β-strand133-13538
α-helix138-14912
α-helix152-1587
α-helix159-1646
α-helix165-17410
α-helix176-1794
β-strand18319
α-helix184-1852
β-strand186-194910
β-strand198-2081110
β-strand20919
β-strand214-219611
β-strand222-223211
α-helix2241
β-strand228-230310
α-helix231-2333
β-strand234-235210
β-strand241-2501010
α-helix254-2563
β-strand257-262611
β-strand270-272311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class I antigenA, Cprotein273Homo sapiensP17693 (AlphaFold model)
Beta-2-microglobulinB, Dprotein100Homo sapiensP61769 (AlphaFold model)
KLPAQFYIL peptideP, Qprotein9
Sequence of entity 1 (A, C), FASTA
>3KYO_1 MHC class I antigen (chains A, C)
SHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSASPRMEPRAPWVEQEGPEYWE
EETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLIRGYERYAYDGK
DYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQR
ADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTF
QKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRW
Sequence of entity 2 (B, D), FASTA
>3KYO_2 Beta-2-microglobulin (chains B, D)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (P, Q), FASTA
>3KYO_3 KLPAQFYIL peptide (chains P, Q)
KLPAQFYIL

Ligands and cofactors

IDNameFormulaCopies
COCobalt (II) ionCo2

Primary citation

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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