Research workbench
Disulfide crosslinked cytochrome P450 reductase inactive
Analyse Disulfide crosslinked cytochrome P450 reductase inactive in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OJX
- Type
- protein
- Length
- 607 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH-cytochrome P450 reductase
- EC
- 1.6.2.4
- UniProt
- P00388
- Ligands
- FMN, FAD, NAP
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-cytochrome P450 reductase (EC 1.6.2.4) | protein | 607 | 38% helix, 20% strand | P00388 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
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 | 922 | 0.82 | 0.83 | 92 | empty |
| 2 | 234 | 0.68 | 0.85 | 34 | FAD |
| 3 | 198 | 0.66 | 0.85 | 35 | FMN |
| 4 | 228 | 0.54 | 0.77 | 28 | NAP |
| 5 | 107 | 0.49 | 0.81 | 24 | empty |
Compared structures
- 3OJX · Disulfide crosslinked cytochrome P450 reductase inactive · the same entry in another collection · chain A against A, TM-score 1.00
- P00388 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (P00388) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P00388
- Elsewhere: RCSB PDB 3OJX · PDBe 3OJX · UniProt P00388
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