MolNFT v1 · #19780 · protein
X-ray structure of a complex NADP+-FERREDOXIN:NADP+ reductase from the cyanobacterium anabaena pcc 7119 at 2.25 ångströms
1QUF · Ferredoxin-NADP+ reductase: “X-ray structure of a complex NADP+-FERREDOXIN:NADP+ reductase from the cyanobacterium anabaena pcc 7119 at…”. X-ray diffraction, 2 ligands (FAD, NAP), 4 pockets (best druggability 0.49). MolNFT v1 #19780…
- PDB
- 1QUF
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- 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
- 4 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-NADP+ reductase (EC 1.18.1.2) | protein | 296 | 26% helix, 28% strand | P21890 |
Ligands and binding sites
- 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
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.49 | 0.77 | 30 | NAP |
| 2 | 131 | 0.46 | 0.77 | 22 | FAD |
| 3 | 53 | 0.32 | 0.77 | 14 | empty |
| 4 | 60 | 0.27 | 0.73 | 22 | empty |
Compared structures
- 1QUF · X-ray structure of a complex NADP+-FERREDOXIN:NADP+ reductase from the cyanobacterium… · 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 A 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 1QUF · PDBe 1QUF · UniProt P21890
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