Research workbench
Structure of the A264H mutant of cytochrome P450 BM3
Analyse Structure of the A264H mutant 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
- 2IJ3
- Type
- protein
- Length
- 907 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 BM3
- EC
- 1.14.14.1
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 BM3 (EC 1.14.14.1) | protein | 453 | 55% helix, 11% strand | P14779 |
| B | Cytochrome P450 BM3 (EC 1.14.14.1) | protein | 454 | 55% helix, 11% 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
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1116 | 0.84 | 0.85 | 119 | HEM |
| 2 | 929 | 0.83 | 0.85 | 92 | HEM |
| 3 | 231 | 0.56 | 0.78 | 33 | empty |
| 4 | 344 | 0.53 | 0.74 | 36 | empty |
| 5 | 176 | 0.50 | 0.77 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 859 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2IJ3 · Structure of the A264H mutant of cytochrome P450 BM3 · the same entry in another collection · chain B against B, 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 A 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 2IJ3 · PDBe 2IJ3 · UniProt P14779
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