MolNFT v1 · #37148 · protein
Crystal structure of cytochrome P450CAM mutant (F87W/Y96F/V247L/C334A)
2FRZ · Cytochrome P450-cam: “Crystal structure of cytochrome P450CAM mutant (F87W/Y96F/V247L/C334A)”. X-ray diffraction, 2 ligands (HEM, K), 7 pockets (best druggability 0.86). MolNFT v1 #37148 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2FRZ
- 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, K
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 50% helix, 10% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.86 | 0.94 | 46 | HEM |
| 2 | 393 | 0.86 | 0.94 | 50 | HEM |
| 3 | 310 | 0.53 | 0.74 | 25 | empty |
| 4 | 62 | 0.39 | 0.80 | 16 | empty |
| 5 | 67 | 0.38 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 120 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2FRZ · Crystal Structure of Cytochrome P450cam mutant (F87W/Y96F/V247L/C334A) · the same entry in another collection · chain A against A, TM-score 1.00
- P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 2FRZ · PDBe 2FRZ · UniProt P00183
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