MolNFT v1 · #187768 · protein
Human cytochrome P450 (cyp) 3A5 ternary complex with azamulin
7SV2: “Human cytochrome P450 (cyp) 3A5 ternary complex with azamulin”. X-ray diffraction, 2 ligands (MWY, HEM). MolNFT v1 #187768 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SV2
- Type
- protein
- Length
- 1,824 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P20815
- Ligands
- MWY, HEM
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 465 | — | P20815 |
| B | — | protein | 465 | — | P20815 |
| C | — | protein | 456 | — | P20815 |
| D | — | protein | 438 | — | P20815 |
Ligands and binding sites
- MWY · (3as,4r,5s,6r,8r,9r,9ar,10r)-6-ethyl-5-hydroxy-4,6,9, 10-tetramethyl-1-oxodecahydro-3A,9-propanocyclopenta[8]annulen-8-yl [(5-amino-1H-1,2,4-triazol-3-yl)sulfanyl]acetate · ligand · 8 copies · chains A, B, C, D
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P20815
- Elsewhere: RCSB PDB 7SV2 · PDBe 7SV2 · UniProt P20815
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