MolNFT v1 · #22537 · protein
Crystal structure of the ferrous cytochrome P450CAM mutant (L358P/C334A)
1T86 · Cytochrome P450-cam: “Crystal structure of the ferrous cytochrome P450CAM mutant (L358P/C334A)”. X-ray diffraction, 3 ligands (HEM, CAM, K), 6 pockets (best druggability 0.86). MolNFT v1 #22537 on GenesisL1: 3D structure, binding…
- PDB
- 1T86
- Type
- protein
- Length
- 812 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450-cam
- EC
- 1.14.15.1
- UniProt
- P00183
- Ligands
- HEM, CAM, K
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome P450-cam (EC 1.14.15.1) | protein | 406 | 52% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CAM · Camphor · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.86 | 0.93 | 51 | HEM, CAM |
| 2 | 443 | 0.86 | 0.93 | 52 | HEM, CAM |
| 3 | 916 | 0.79 | 0.81 | 73 | empty |
| 4 | 117 | 0.52 | 0.82 | 23 | empty |
| 5 | 89 | 0.48 | 0.81 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 721 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1T86 · Crystal Structure of the Ferrous Cytochrome P450cam Mutant (L358P/C334A) · the same entry in another collection · chain A against A, TM-score 1.00
- P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · a predicted model of the same protein · chain B 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 1T86 · PDBe 1T86 · UniProt P00183
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