Research workbench
Crystal structure of RQA_M phosphopeptide bound to human class I MHC HLA-A2
Analyse Crystal structure of RQA_M phosphopeptide bound to human class I MHC HLA-A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BH8
- Type
- protein
- Length
- 384 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01892, P61769, P33241
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 274 | — | P01892 |
| B | — | protein | 100 | — | P61769 |
| C | — | protein | 10 | — | P33241 |
Compared structures
- 3BH8 · Crystal Structure of RQA_M Phosphopeptide Bound to HUMAN Class I MHC HLA-A2 · the same entry in another collection · chain A against A, TM-score 1.00
- P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P33241 · AlphaFold monomer V2.0 prediction for lymphocyte-specific protein 1 (P33241) · a predicted model of the same protein · chain C against A, TM-score 0.36
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01892
- Every structure of UniProt P61769
- Every structure of UniProt P33241
- Elsewhere: RCSB PDB 3BH8 · PDBe 3BH8 · UniProt P01892 · UniProt P61769 · UniProt P33241
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