MolNFT v1 · #118707 · protein
Wild type human cypor
5FA6 · NADPH--cytochrome P450 reductase: “Wild type human cypor”. X-ray diffraction, 3 ligands (FMN, FAD, NAP), 10 pockets (best druggability 0.85). MolNFT v1 #118707 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FA6
- Type
- protein
- Length
- 1,208 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
- P16435
- Ligands
- FMN, FAD, NAP
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 606 | 38% helix, 21% strand | P16435 |
| B | NADPH--cytochrome P450 reductase (EC 1.6.2.4) | protein | 602 | 37% helix, 22% strand | P16435 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NAP · Nadp 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
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 889 | 0.85 | 0.87 | 122 | FMN |
| 2 | 486 | 0.80 | 0.88 | 68 | empty |
| 3 | 348 | 0.77 | 0.87 | 54 | FMN |
| 4 | 405 | 0.65 | 0.79 | 54 | empty |
| 5 | 244 | 0.60 | 0.80 | 30 | NAP |
Interfaces
1 interface between chains.
- A–B · 470 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P16435
- Elsewhere: RCSB PDB 5FA6 · PDBe 5FA6 · UniProt P16435
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