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.
Explore 2CLV in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-150 | 13 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-179 | 16 | |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 2 |
| β-strand | 198-208 | 11 | 2 |
| β-strand | 214-219 | 6 | 3 |
| β-strand | 222-223 | 2 | 3 |
| β-strand | 229-230 | 2 | 2 |
| β-strand | 234-235 | 2 | 2 |
| β-strand | 241-250 | 10 | 2 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 3 |
| β-strand | 270-272 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 4 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 5 |
| β-strand | 21-30 | 10 | 5 |
| β-strand | 31 | 1 | 4 |
| β-strand | 36-41 | 6 | 6 |
| β-strand | 44-45 | 2 | 6 |
| β-strand | 50-51 | 2 | 5 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 5 |
| β-strand | 62-70 | 9 | 5 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 91-94 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 7 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 7 |
| β-strand | 31-37 | 7 | 7 |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-85 | 29 | |
| β-strand | 94-103 | 10 | 7 |
| β-strand | 109-118 | 10 | 7 |
| β-strand | 121-126 | 6 | 7 |
| β-strand | 133-135 | 3 | 7 |
| α-helix | 138-150 | 13 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-179 | 16 | |
| β-strand | 183 | 1 | 8 |
| β-strand | 186-193 | 8 | 9 |
| β-strand | 198-208 | 11 | 9 |
| β-strand | 209 | 1 | 8 |
| β-strand | 214-219 | 6 | 10 |
| β-strand | 222-223 | 2 | 10 |
| β-strand | 228-230 | 3 | 9 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 9 |
| β-strand | 241-250 | 10 | 9 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 10 |
| β-strand | 270-272 | 3 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2 | 1 | |
| β-strand | 3 | 1 | 11 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 12 |
| β-strand | 21-30 | 10 | 12 |
| β-strand | 31 | 1 | 11 |
| β-strand | 36-41 | 6 | 13 |
| β-strand | 44-45 | 2 | 13 |
| β-strand | 50-51 | 2 | 12 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 12 |
| β-strand | 62-70 | 9 | 12 |
| β-strand | 78-83 | 6 | 13 |
| β-strand | 91-94 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class I histocompatibility antigen, K-B alpha chain | A, H | protein | 279 | MUS MUSCULUS | P01901 (AlphaFold model) |
| Beta-2 microglobulin | B, P | protein | 99 | MUS MUSCULUS | P01887 (AlphaFold model) |
| RBM5 protein | C, M | protein | 8 | MUS MUSCULUS | Q91YE7 (AlphaFold model) |
>2CLV_1 H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN (chains A, H) GPHSLRYFVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRYEPRARWMEQEGPEYW ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG CDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLL RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPS
>2CLV_2 BETA-2 MICROGLOBULIN (chains B, P) IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
>2CLV_3 RBM5 PROTEIN (chains C, M) SQYYYNSL
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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