MolNFT v1 · #137687 · protein
Nicotinamide soak of Y316S mutant of corn root FERREDOXIN:NADP+ reductase in alternate space group
5VW9 · Ferredoxin--NADP reductase: “Nicotinamide soak of Y316S mutant of corn root FERREDOXIN:NADP+ reductase in alternate space group”. X-ray diffraction, 3 ligands (FAD, NCA, MG), 2 pockets (best druggability 0.58). MolNFT v1 #137687 on…
- PDB
- 5VW9
- Type
- protein
- Length
- 309 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
- Q41736
- Ligands
- FAD, NCA, MG
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 309 | 27% helix, 29% strand | Q41736 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NCA · Nicotinamide · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.58 | 0.77 | 40 | FAD, NCA, ACT |
| 2 | 76 | 0.33 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5VW9 · Nicotinamide soak of Y316S mutant of corn root ferredoxin:NADP+ reductase in alternate… · 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 Q41736
- Elsewhere: RCSB PDB 5VW9 · PDBe 5VW9 · UniProt Q41736
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