MolNFT v1 · #83734 · protein
Crystal structure of P450CAM
3WRM · Camphor 5-monooxygenase: “Crystal structure of P450CAM”. X-ray diffraction, 3 ligands (HEM, CAM, K), 4 pockets (best druggability 0.87). MolNFT v1 #83734 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3WRM
- Type
- protein
- Length
- 810 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camphor 5-monooxygenase
- EC
- 1.14.15.1
- UniProt
- P00183
- Ligands
- HEM, CAM, K
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 405 | 53% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, F
- CAM · Camphor · ligand · 2 copies · chains A, F
- K · Potassium ion · metal · 2 copies · chains A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.87 | 0.94 | 49 | HEM, CAM |
| 2 | 434 | 0.86 | 0.93 | 49 | HEM, CAM |
| 3 | 711 | 0.70 | 0.77 | 54 | empty |
| 4 | 69 | 0.31 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–F · 323 Ų buried · 9 hydrogen bonds · protein-protein
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 P00183
- Elsewhere: RCSB PDB 3WRM · PDBe 3WRM · UniProt P00183
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.