Research workbench
Cytochrome P450 BM3 mutant in complex with palmitic acid
Analyse Cytochrome P450 BM3 mutant in complex with palmitic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UWH
- Type
- protein
- Length
- 2,748 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- BACILLUS MEGATERIUM
- Molecule
- Bifunctional P-450\: NADPH-P450 reductase
- EC
- 1.14.14.1
- UniProt
- P14779
- Ligands
- HEM, PLM
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · resolution 2.8 · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Bifunctional P-450\: NADPH-P450 reductase (EC 1.14.14.1) | protein | 458 | 53% helix, 11% strand | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 6 copies · chains A, B, C, D, E, F
- PLM · Palmitic acid · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.89 | 0.94 | 77 | HEM, PLM |
| 2 | 584 | 0.88 | 0.94 | 82 | HEM, PLM |
| 3 | 634 | 0.88 | 0.93 | 83 | HEM, PLM |
| 4 | 615 | 0.88 | 0.93 | 84 | HEM, PLM |
| 5 | 597 | 0.88 | 0.93 | 81 | HEM, PLM |
Interfaces
8 interfaces between chains.
- D–E · 1098 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 528 Ų buried · 2 hydrogen bonds · protein-protein
- C–F · 481 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 426 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 415 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2UWH · Cytochrome P450 BM3 mutant in complex with palmitic acid · the same entry in another collection · chain F against F, 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 F against A, TM-score 0.98
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 2UWH · PDBe 2UWH · UniProt P14779
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