Research workbench
Cytochrome P450 reductase in complex with NADPH from candida tropicalis
Analyse Cytochrome P450 reductase in complex with NADPH from candida tropicalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T1T
- Type
- protein
- Length
- 1,270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH--cytochrome P450 reductase
- EC
- 1.6.2.4
- UniProt
- Q5PXH3
- Ligands
- FAD, FMN, NDP
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 635 | 36% helix, 21% strand | Q5PXH3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1092 | 0.82 | 0.83 | 125 | FAD, FMN |
| 2 | 759 | 0.78 | 0.82 | 74 | empty |
| 3 | 724 | 0.77 | 0.81 | 67 | empty |
| 4 | 486 | 0.75 | 0.83 | 53 | FMN |
| 5 | 588 | 0.71 | 0.80 | 60 | NDP |
Interfaces
1 interface between chains.
- A–B · 1645 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 6T1T · Cytochrome P450 reductase in complex with NADPH from Candida tropicalis · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5PXH3
- Elsewhere: RCSB PDB 6T1T · PDBe 6T1T · UniProt Q5PXH3
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