MolNFT v1 · #175406 · protein
The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P450(CAM)
7CPP: “The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome…”. X-ray diffraction, 2 ligands (HEM, NCM). MolNFT v1 #175406 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7CPP
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00183
- Ligands
- HEM, NCM
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 405 | — | P00183 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P00183
- Elsewhere: RCSB PDB 7CPP · PDBe 7CPP · UniProt P00183
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