MolNFT v1 · #25872 · protein
Ferredoxin-NADP reductase (mutation: Y 303 W) complexed with NADP by cocrystallization
1W87: “Ferredoxin-NADP reductase (mutation: Y 303 W) complexed with NADP by cocrystallization”. X-ray diffraction, 2 ligands (FAD, NAP), 1 pocket (best druggability 0.83). MolNFT v1 #25872 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1W87
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-NADP reductase
- EC
- 1.18.1.2
- UniProt
- P21890
- Ligands
- FAD, NAP
- Pockets
- 1 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ferredoxin-NADP reductase (EC 1.18.1.2) | protein | 295 | 26% helix, 29% strand | P21890 |
Ligands and binding sites
- 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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.83 | 0.84 | 100 | FAD, NAP |
Interfaces
1 interface between chains.
- A–B · 520 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1W87 · Ferredoxin-NADP reductase (mutation: Y 303 W) complexed with NADP by cocrystallization · the same entry in another collection · chain A against A, TM-score 1.00
- P21890 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (P21890) · a predicted model of the same protein · chain B 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 P21890
- Elsewhere: RCSB PDB 1W87 · PDBe 1W87 · UniProt P21890
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