Research workbench
Crystal structure of the A264C mutant heme domain of cytochrome P450 BM3
Analyse Crystal structure of the A264C mutant heme domain of cytochrome P450 BM3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EKB
- Type
- protein
- Length
- 899 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450(BM-3)
- EC
- 1.14.14.1
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 7 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450(BM-3) (EC 1.14.14.1) | protein | 442 | 50% helix, 12% strand | P14779 |
| B | Cytochrome P450(BM-3) (EC 1.14.14.1) | protein | 457 | 51% helix, 12% strand | P14779 |
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
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 648 | 0.88 | 0.92 | 89 | HEM |
| 2 | 885 | 0.87 | 0.88 | 94 | HEM |
| 3 | 138 | 0.60 | 0.85 | 24 | empty |
| 4 | 180 | 0.56 | 0.81 | 26 | empty |
| 5 | 242 | 0.48 | 0.74 | 33 | empty |
Compared structures
- 3EKB · Crystal structure of the A264C mutant heme domain of cytochrome P450 BM3 · the same entry in another collection · chain A against A, TM-score 1.00
- P14779 · AlphaFold monomer V2.0 prediction for bifunctional cytochrome P450/NADPH--P450 reductase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P14779
- Elsewhere: RCSB PDB 3EKB · PDBe 3EKB · UniProt P14779
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