MolNFT v1 · #17679 · protein
F393Y mutant heme domain of flavocytochrome P450 BM3
1P0X · Bifunctional P-450:NADPH-P450 reductase: “F393Y mutant heme domain of flavocytochrome P450 BM3”. X-ray diffraction, 1 ligand (HEM), 6 pockets (best druggability 0.86). MolNFT v1 #17679 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1P0X
- Type
- protein
- Length
- 889 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional P-450:NADPH-P450 reductase
- EC
- 1.14.14.1
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional P-450:NADPH-P450 reductase (EC 1.14.14.1) | protein | 441 | 54% helix, 11% strand | P14779 |
| B | Bifunctional P-450:NADPH-P450 reductase (EC 1.14.14.1) | protein | 448 | 56% 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
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.86 | 0.87 | 103 | HEM |
| 2 | 1187 | 0.82 | 0.83 | 109 | HEM |
| 3 | 482 | 0.60 | 0.75 | 45 | empty |
| 4 | 172 | 0.52 | 0.79 | 27 | empty |
| 5 | 239 | 0.47 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 472 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1P0X · F393Y mutant heme domain of flavocytochrome 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 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 1P0X · PDBe 1P0X · UniProt P14779
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