9PBG: TCR 19.2 complex with YEIH-HLA B*27:05

TCR 19.2 complex with YEIH-HLA B*27:05. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Mar 2026.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Homo sapiens, Escherichia coli
Chains
5
Atoms
6,848
Mol. weight
96.69 kDa
Ligands
NAG
Released
18 Mar 2026

Explore 9PBG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PBG contains 25 α-helices and 71 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-helix50-545
α-helix57-8529
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-15013
α-helix152-1587
α-helix159-1635
α-helix164-17411
α-helix176-1794
α-helix1821
β-strand18312
α-helix184-1852
β-strand186-19383
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
α-helix225-2273
β-strand229-23023
β-strand234-23523
β-strand241-250103
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 D: 5 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand5-848
β-strand11-1559
β-strand20-2678
β-strand31-3999
β-strand45-5289
β-strand57-6048
β-strand63-6868
β-strand73-7868
α-helix83-853
β-strand87-96109
β-strand103-10759
β-strand111-11669
α-helix117-1182
β-strand125-130610
β-strand138-143610
α-helix151-1544
β-strand159-161310
α-helix162-1643
β-strand165-169510
β-strand174-1831010
α-helix190-1945
Chain E: 6 helices, 25 β-strands
ElementResiduesLengthSheet
β-strand5-7311
β-strand10-14512
β-strand19-24611
β-strand31-38812
β-strand42-50912
β-strand53-57512
β-strand64-68511
β-strand74-78511
α-helix83-853
β-strand87-94812
β-strand104-105212
β-strand109-114612
α-helix117-1193
β-strand121113
β-strand124-128514
β-strand129110
α-helix130-1312
α-helix132-1376
β-strand140-1501114
β-strand151113
β-strand155-161715
β-strand164-166315
β-strand170-172314
β-strand177-178214
β-strand188-1971014
α-helix198-2014
β-strand207-214815
β-strand217116
α-helix228-2292
β-strand231116
β-strand233-240815

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class I antigenAprotein279Homo sapiensA3F718 (AlphaFold model)
Beta-2-microglobulinBprotein100Homo sapiensP61769 (AlphaFold model)
UPF0324 inner membrane protein YeiHCprotein9Escherichia coliP62723 (AlphaFold model)
TCR 19.2 alpha chainDprotein210Homo sapiens
TCR19.2 beta chainEprotein244Homo sapiens
Sequence of entity 1 (A), FASTA
>9PBG_1 MHC class I antigen (chains A)
MGSHSMRYFHTSVSRPGRGEPRFITVGYVDDTLFVRFDSDAASPREEPRAPWIEQEGPEY
WDRETQISKAKAQTDREDLRTLLRYYNQSEAGSHTLQNMYGCDVGPDGRLLRGYHQDAYD
GKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGECVEWLRRYLENGKETL
QRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDR
TFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSS
Sequence of entity 2 (B), FASTA
>9PBG_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C), FASTA
>9PBG_3 UPF0324 inner membrane protein YeiH (chains C)
LRVMMLAPF
Sequence of entity 4 (D), FASTA
>9PBG_4 TCR 19.2 alpha chain (chains D)
KQEVTQIPAALSVPEGENLVLNCSFTDSAIYNLQWFRQDPGKGLTSLLLIQSSQREQTSG
RLNASLDKSSGRSTLYIAASQPGDSATYLCGIALIGSGAGSYQLTFGKGTKLSVIPNIQN
PDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVA
WSNKSDFACANAFNNSIIPEDTFFPSPESS
Sequence of entity 5 (E), FASTA
>9PBG_5 TCR19.2 beta chain (chains E)
DSGVTQTPKHLITATGQRVTLRCSPRSGDLSVYWYQQSLDQGLQFLIQYYNGEERAKGNI
LERFSAQQFPDLHSELNLSSLELGDSALYFCASSPATYSTDTQYFGPGTRLTVLEDLKNV
FPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQ
PALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAW
GRAD

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Water and common crystallization additives (GOL) are not listed.

Primary citation

Deep peptide recognition profiling decodes TCR specificity and enables disease-associated antigen discovery. Wang, N., Yeh, H., Lai, B. et al. Nat Biotechnol (2026). DOI 10.1038/s41587-026-03128-x · PubMed

Other PDB entries of the same protein (UniProt A3F718 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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