Research workbench
Structure of cyanide and camphor bound P450CAM mutant L358A
Analyse Structure of cyanide and camphor bound P450CAM mutant L358A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L4D
- 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, CYN
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 405 | 52% helix, 10% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CAM · Camphor · ligand · chains A
- K · Potassium ion · metal · 2 copies · chains A
- CYN · Cyanide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 422 | 0.86 | 0.94 | 51 | HEM, CYN, CAM |
| 2 | 94 | 0.42 | 0.79 | 17 | empty |
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 4L4D · PDBe 4L4D · UniProt P00183
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