Research workbench
Crystal structure of P450CAM
Analyse Crystal structure of P450CAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WRK
- Type
- protein
- Length
- 783 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
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 391 | 51% helix, 11% strand | P00183 |
| D | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 392 | 51% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, D
- CAM · Camphor · ligand · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 780 | 0.79 | 0.82 | 71 | HEM, CAM |
| 2 | 786 | 0.78 | 0.82 | 76 | HEM, CAM |
| 3 | 480 | 0.75 | 0.84 | 66 | empty |
| 4 | 181 | 0.44 | 0.74 | 26 | empty |
| 5 | 60 | 0.34 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–D · 669 Ų buried · 14 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 3WRK · PDBe 3WRK · UniProt P00183
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