6TDS: MHC class I antigen

Crystal structure of the disulfide engineered HLA-A0201 molecule without peptide bound after NaCl wash. Determined by X-ray diffraction at 1.7 Å resolution. Released 25 Mar 2020.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
4
Atoms
6,591
Mol. weight
88.67 kDa
Released
25 Mar 2020

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

Secondary structure: helices and β-sheets

6TDS contains 26 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-helix57-8529
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-1587
α-helix159-1635
α-helix164-17411
α-helix176-1794
β-strand18312
β-strand186-19383
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
α-helix225-2273
β-strand229-23023
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27344
Chain B: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand415
α-helix5-62
β-strand7-1266
β-strand22-31106
β-strand3215
β-strand37-4267
β-strand45-4627
β-strand51-5226
α-helix53-553
β-strand56-5726
β-strand63-7196
β-strand79-8467
β-strand92-9547
Chain C: 10 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
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-helix159-1635
α-helix164-17411
α-helix176-1794
β-strand18319
β-strand186-193810
β-strand198-2081110
β-strand20919
β-strand214-219611
β-strand222-223211
α-helix225-2273
β-strand229-230210
α-helix231-2333
β-strand234-235210
β-strand241-2501010
α-helix254-2563
β-strand257-262611
β-strand270-273411
Chain D: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand4112
α-helix5-62
β-strand7-12613
β-strand22-311013
β-strand32112
β-strand36-42714
β-strand45-46214
α-helix471
β-strand51-52213
α-helix53-553
β-strand56-57213
β-strand63-71913
β-strand79-85714
β-strand92-95414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class I antigenA, Cprotein276Homo sapiensF6IQS1 (AlphaFold model)
Beta-2-microglobulinB, Dprotein100Homo sapiensP61769 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>6TDS_1 MHC class I antigen (chains A, C)
AGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY
WDGETRKVKAHSQTHRVDLGTLRGCYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD
GKDYIALKEDLRSWTAADMCAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL
QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWVAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE
Sequence of entity 2 (B, D), FASTA
>6TDS_2 Beta-2-microglobulin (chains B, D)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Primary citation

Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection. Anjanappa, R., Garcia-Alai, M., Kopicki, J.D. et al. Nat Commun (2020) 11:1314-1314. DOI 10.1038/s41467-020-14862-4 · PubMed

Other PDB entries of the same protein (UniProt F6IQS1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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