2CLV: MHC Class I Natural Mutant H-2Kbm8 Heavy Chain

MHC Class I Natural Mutant H-2Kbm8 Heavy Chain Complexed With beta-2 Microglobulin and pBM8 peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 14 Jun 2006.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
MUS MUSCULUS
Chains
6
Atoms
6,950
Mol. weight
89.64 kDa
Released
14 Jun 2006

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

Secondary structure: helices and β-sheets

2CLV contains 24 α-helices and 58 β-strands across 5 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: 9 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand3-12101
α-helix201
β-strand21-2881
β-strand31-3771
β-strand46-4721
α-helix50-545
α-helix57-8428
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-15013
α-helix152-1587
α-helix159-1635
α-helix164-17916
α-helix184-1852
β-strand186-19382
β-strand198-208112
β-strand214-21963
β-strand222-22323
β-strand229-23022
β-strand234-23522
β-strand241-250102
α-helix254-2563
β-strand257-26263
β-strand270-27233
Chain B: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand314
α-helix4-52
β-strand6-1165
β-strand21-30105
β-strand3114
β-strand36-4166
β-strand44-4526
β-strand50-5125
α-helix52-543
β-strand55-5625
β-strand62-7095
β-strand78-8366
β-strand91-9446
Chain H: 9 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12107
α-helix201
β-strand21-2887
β-strand31-3777
β-strand46-4727
α-helix50-523
α-helix57-8529
β-strand94-103107
β-strand109-118107
β-strand121-12667
β-strand133-13537
α-helix138-15013
α-helix152-1587
α-helix159-1635
α-helix164-17916
β-strand18318
β-strand186-19389
β-strand198-208119
β-strand20918
β-strand214-219610
β-strand222-223210
β-strand228-23039
α-helix231-2333
β-strand234-23529
β-strand241-250109
α-helix254-2563
β-strand257-262610
β-strand270-272310
Chain M: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix5-73
Chain P: 3 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix21
β-strand3111
α-helix4-52
β-strand6-11612
β-strand21-301012
β-strand31111
β-strand36-41613
β-strand44-45213
β-strand50-51212
α-helix52-543
β-strand55-56212
β-strand62-70912
β-strand78-83613
β-strand91-94413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class I histocompatibility antigen, K-B alpha chainA, Hprotein279MUS MUSCULUSP01901 (AlphaFold model)
Beta-2 microglobulinB, Pprotein99MUS MUSCULUSP01887 (AlphaFold model)
RBM5 proteinC, Mprotein8MUS MUSCULUSQ91YE7 (AlphaFold model)
Sequence of entity 1 (A, H), FASTA
>2CLV_1 H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN (chains A, H)
GPHSLRYFVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRYEPRARWMEQEGPEYW
ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG
CDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLL
RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT
FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPS
Sequence of entity 2 (B, P), FASTA
>2CLV_2 BETA-2 MICROGLOBULIN (chains B, P)
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
Sequence of entity 3 (C, M), FASTA
>2CLV_3 RBM5 PROTEIN (chains C, M)
SQYYYNSL

Primary citation

Distinct orientation of the alloreactive monoclonal CD8 T cell activation program by three different peptide/MHC complexes. Auphan-Anezin, N., Mazza, C., Guimezanes, A. et al. Eur J Immunol (2006) 36:1856-1866. DOI 10.1002/eji.200635895 · PubMed

Other PDB entries of the same protein (UniProt P01901 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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