6P2C: PDB entry 6P2C

Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation. Determined by X-ray diffraction at 1.4 Å resolution. Released 16 Oct 2019.

Method
X-ray diffraction
Resolution
1.4 Å
Organisms
Homo sapiens, Human immunodeficiency virus 1
Chains
3
Atoms
3,450
Mol. weight
45.96 kDa
Released
16 Oct 2019

Explore 6P2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6P2C contains 16 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.

Chain A: 12 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-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-1587
α-helix159-1646
α-helix165-17410
α-helix176-1794
α-helix1821
β-strand18312
α-helix184-1852
β-strand186-19383
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
β-strand228-23033
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chain B: 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: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-63

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class I histocompatibility antigen, B-8 alpha chainAprotein276Homo sapiensP01889 (AlphaFold model)
Beta-2-microglobulinBprotein99Homo sapiensP61769 (AlphaFold model)
MHC I-peptideCprotein20Human immunodeficiency virus 1
Sequence of entity 1 (A), FASTA
>6P2C_1 HLA class I histocompatibility antigen, B-8 alpha chain (chains A)
GSHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYW
DRNTQIFKTNTQTDRCSLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDG
KDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKDTLE
RADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B), FASTA
>6P2C_2 Beta-2-microglobulin (chains B)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C), FASTA
>6P2C_3 MHC I-peptide (chains C)
RARARARARARAAAKKKYCL

Primary citation

ERAP1 enzyme-mediated trimming and structural analyses of MHC I-bound precursor peptides yield novel insights into antigen processing and presentation. Li, L., Batliwala, M., Bouvier, M. J Biol Chem (2019) 294:18534-18544. DOI 10.1074/jbc.RA119.010102 · PubMed

Other PDB entries of the same protein (UniProt P01889 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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