Research workbench
Crystal structure of HLA-B*57:01 with an HIV peptide rkv
Analyse Crystal structure of HLA-B*57:01 with an HIV peptide rkv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BXQ
- Type
- protein
- Length
- 384 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV peptide rkv; MHC class I antigen; Beta-2-microglobulin
- UniProt
- U6BR87, P61769
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV peptide rkv | protein | 8 | 0% helix, 0% strand | — |
| B | MHC class I antigen | protein | 276 | 26% helix, 39% strand | U6BR87 |
| C | Beta-2-microglobulin | protein | 100 | 0% helix, 49% strand | P61769 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.70 | 0.78 | 56 | empty |
| 2 | 143 | 0.64 | 0.86 | 24 | empty |
| 3 | 86 | 0.42 | 0.79 | 21 | empty |
| 4 | 81 | 0.39 | 0.78 | 18 | empty |
| 5 | 61 | 0.36 | 0.78 | 15 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1375 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 964 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 U6BR87
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 6BXQ · PDBe 6BXQ · UniProt U6BR87 · UniProt P61769
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