1XR9: HLA-B*1501

Crystal Structures of HLA-B*1501 in Complex with Peptides from Human UbcH6 and Epstein-Barr Virus EBNA-3. Determined by X-ray diffraction at 1.79 Å resolution. Released 14 Apr 2005.

Method
X-ray diffraction
Resolution
1.79 Å
Organism
Homo sapiens
Chains
3
Atoms
3,917
Mol. weight
44.95 kDa
Ligands
URE
Released
14 Apr 2005

Explore 1XR9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1XR9 contains 15 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-helix152-16110
α-helix163-17412
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
α-helix231-2333
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
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: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-54

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class I histocompatibility antigen, B-15 alpha chainAprotein276Homo sapiensP01889 (AlphaFold model)
Beta-2-microglobulinBprotein99Homo sapiensP61769 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 E1Cprotein9P51965 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1XR9_1 HLA class I histocompatibility antigen, B-15 alpha chain (chains A)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYW
DRETQISKTNTQTYRESLRNLRGYYNQSEAGSHTLQRMYGCDVGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQWRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B), FASTA
>1XR9_2 Beta-2-microglobulin (chains B)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C), FASTA
>1XR9_3 Ubiquitin-conjugating enzyme E2 E1 (chains C)
ILGPPGSVY

Ligands and cofactors

IDNameFormulaCopies
UREUreaC H4 N2 O1

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

Crystal structures of two peptide-HLA-B*1501 complexes; structural characterization of the HLA-B62 supertype. Roder, G., Blicher, T., Justesen, S. et al. Acta Crystallogr D Biol Crystallogr (2006) 62:1300-1310. DOI 10.1107/S0907444906027636 · PubMed

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

Browse structure collections

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