Research workbench
Crystal structure of camphor-bound P450CAM at low [K+]
Analyse Crystal structure of camphor-bound P450CAM at low [K+] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L63
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- 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
- 1 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 405 | 51% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CAM · Camphor · ligand · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 446 | 0.87 | 0.94 | 48 | HEM, CAM |
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 3L63 · PDBe 3L63 · UniProt P00183
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