MolNFT v1 · #28846 · protein
T268N mutant cytochrome domain of flavocytochrome P450 BM3
1YQP · Bifunctional P-450:NADPH-P450 reductase: “T268N mutant cytochrome domain of flavocytochrome P450 BM3”. X-ray diffraction, 1 ligand (HEM), 8 pockets (best druggability 0.86). MolNFT v1 #28846 on GenesisL1: 3D structure, binding sites…
- PDB
- 1YQP
- Type
- protein
- Length
- 882 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, 1.6.2.4
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bifunctional P-450:NADPH-P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 441 | 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
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.86 | 0.87 | 100 | HEM |
| 2 | 965 | 0.82 | 0.83 | 97 | HEM |
| 3 | 465 | 0.60 | 0.75 | 43 | empty |
| 4 | 172 | 0.58 | 0.82 | 29 | empty |
| 5 | 249 | 0.57 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 468 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1YQP · T268N mutant cytochrome 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 1YQP · PDBe 1YQP · UniProt P14779
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