1TVB: Melanoma Antigen gp100(209-217)

Crystal structure of Melanoma Antigen gp100(209-217) Bound to Human Class I MHC HLA-A2. Determined by X-ray diffraction at 1.8 Å resolution. Released 19 Apr 2005.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
6
Atoms
7,378
Mol. weight
91.5 kDa
Released
19 Apr 2005

Explore 1TVB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TVB contains 32 α-helices and 60 β-strands across 6 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-helix159-1635
α-helix164-17411
α-helix176-1794
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
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-strand315
α-helix4-52
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
β-strand50-5126
α-helix52-543
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-32
α-helix6-83
Chain D: 12 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
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-strand133-13428
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
α-helix225-2273
β-strand229-230210
α-helix231-2333
β-strand234-235210
β-strand241-2501010
α-helix254-2563
β-strand257-262611
β-strand270-272311
Chain E: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
α-helix4-52
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
α-helix461
β-strand50-51213
α-helix52-543
β-strand55-56213
β-strand62-70913
β-strand78-83614
β-strand91-94414
Chain F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix5-84

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class I histocompatibility antigen, A-2 alpha chainA, Dprotein275Homo sapiensP04439 (AlphaFold model)
Beta-2-microglobulinB, Eprotein100Homo sapiensP61769 (AlphaFold model)
epitope of Melanocyte protein Pmel 17C, Fprotein9P40967 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1TVB_1 HLA class I histocompatibility antigen, A-2 alpha chain (chains A, D)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE
Sequence of entity 2 (B, E), FASTA
>1TVB_2 Beta-2-microglobulin (chains B, E)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, F), FASTA
>1TVB_3 epitope of Melanocyte protein Pmel 17 (chains C, F)
ITDQVPFSV

Primary citation

Increased Immunogenicity of an Anchor-Modified Tumor-Associated Antigen Is Due to the Enhanced Stability of the Peptide/MHC Complex: Implications for Vaccine Design. Borbulevych, O.Y., Baxter, T.K., Yu, Z. et al. J Immunol (2005) 174:4812-4820. 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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