MolNFT v1 · #6144 · protein
Ferredoxin reductase (BPHA4)-NADH complex
1F3P: “Ferredoxin reductase (BPHA4)-NADH complex”. X-ray diffraction, 2 ligands (FAD, NAD), 2 pockets (best druggability 0.82). MolNFT v1 #6144 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1F3P
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin reductase
- EC
- 1.14.-.-
- UniProt
- Q52437
- Ligands
- FAD, NAD
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin reductase (EC 1.14.-.-) | protein | 401 | 26% helix, 30% strand | Q52437 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.82 | 0.86 | 84 | FAD, NAD |
| 2 | 139 | 0.50 | 0.79 | 17 | empty |
Compared structures
- 1F3P · Ferredoxin reductase (BPHA4)-NADH complex · 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 Q52437
- Elsewhere: RCSB PDB 1F3P · PDBe 1F3P · UniProt Q52437
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