Research workbench
Crystal structure of cytochrome P450CAM mutant (F87W/Y96F)
Analyse Crystal structure of cytochrome P450CAM mutant (F87W/Y96F) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C8J
- Type
- protein
- Length
- 810 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
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 51% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
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 | 426 | 0.86 | 0.94 | 48 | HEM |
| 2 | 431 | 0.86 | 0.94 | 49 | HEM |
| 3 | 329 | 0.55 | 0.75 | 26 | empty |
| 4 | 80 | 0.39 | 0.78 | 17 | empty |
| 5 | 67 | 0.37 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 117 Ų buried · 3 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 1C8J · PDBe 1C8J · UniProt P00183
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