2BCK: HLA-A*2402

Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide. Determined by X-ray diffraction at 2.8 Å resolution. Released 10 Jan 2006.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
6
Atoms
6,614
Mol. weight
94.39 kDa
Released
10 Jan 2006

Explore 2BCK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BCK contains 24 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-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-1576
α-helix158-1647
α-helix165-1739
α-helix176-1794
β-strand18312
α-helix184-1852
β-strand188-19363
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
α-helix225-2273
β-strand228-23033
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chain B: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
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: 9 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
α-helix201
β-strand21-2888
β-strand31-3778
β-strand46-4728
α-helix57-8529
β-strand94-103108
β-strand109-118108
β-strand122-12658
β-strand133-13538
α-helix138-14912
α-helix152-1587
α-helix159-1635
α-helix164-17411
α-helix176-1794
β-strand18319
α-helix184-1852
β-strand186-193810
β-strand198-2081110
β-strand20919
β-strand214-219611
β-strand222-223211
β-strand228-230310
α-helix231-2333
β-strand234-235210
β-strand241-2501010
β-strand257-262611
β-strand270-273411
Chain E: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
α-helix461
β-strand50-51213
α-helix52-543
β-strand56113
β-strand62-70913
β-strand78-83614
β-strand91-94414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class I histocompatibility antigen, A-24 alpha chainA, Dprotein294Homo sapiensP04439 (AlphaFold model)
Beta-2-microglobulinB, Eprotein100Homo sapiensP61769 (AlphaFold model)
Telomerase reverse transcriptaseC, Fprotein9O14746 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>2BCK_1 HLA class I histocompatibility antigen, A-24 alpha chain (chains A, D)
GSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DEETGKVKAHSQTDRENLRIALRYYNQSEAGSHTLQMMFGCDVGSDGRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQITKRKWEAAHVAEQQRAYLEGTCVDGLRRYLENGKETLQ
RTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPGSGGGLNDIFEAQKIEWH
Sequence of entity 2 (B, E), FASTA
>2BCK_2 Beta-2-microglobulin (chains B, E)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, F), FASTA
>2BCK_3 Telomerase reverse transcriptase (chains C, F)
VYGFVRACL

Primary citation

Crystal structure of HLA-A*2402 complexed with a telomerase peptide. Cole, D.K., Rizkallah, P.J., Gao, F. et al. Eur J Immunol (2006) 36:170-179. DOI 10.1002/eji.200535424 · PubMed

Other PDB entries of the same protein (UniProt P04439 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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