MolNFT v2 · #145466 · protein
Crystal Structure of HLA-B*57:01 with a modified HIV peptide RKV-Kyn
6BXP: “Crystal Structure of HLA-B*57:01 with a modified HIV peptide RKV-Kyn”. X-ray diffraction at 1.45. MolNFT v2 #145466 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BXP
- Type
- protein
- Length
- 380 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.45
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- UniProt
- P18465, P61769
Structure
x-ray diffraction · resolution 1.45 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 275 | — | P18465 |
| B | — | protein | 99 | — | P61769 |
| C | — | protein | 6 | — | — |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BXP · Crystal structure of HLA-B*57:01 with a modified HIV peptide rkv-kyn · 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 0.99
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 P18465
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 6BXP · PDBe 6BXP · UniProt P18465 · UniProt P61769
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