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Crystal structure of cytochrome P450 2B4 F429H in complex with 4-cpi
Analyse Crystal structure of cytochrome P450 2B4 F429H in complex with 4-cpi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MGJ
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 2B4
- EC
- 1.14.14.1
- UniProt
- P00178
- Ligands
- HEM, CPZ
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 2B4 (EC 1.14.14.1) | protein | 452 | 54% helix, 8% strand | P00178 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CPZ · 4-(4-chlorophenyl)imidazole · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.87 | 0.94 | 54 | HEM, CPZ |
| 2 | 68 | 0.73 | 0.96 | 14 | empty |
| 3 | 260 | 0.66 | 0.83 | 27 | empty |
| 4 | 70 | 0.41 | 0.80 | 19 | empty |
| 5 | 97 | 0.39 | 0.76 | 27 | 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 P00178
- Elsewhere: RCSB PDB 4MGJ · PDBe 4MGJ · UniProt P00178
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