Research workbench

NADPH soak of Y316A mutant of corn root FERREDOXIN:NADP+ reductase

Analyse NADPH soak of Y316A mutant of corn root FERREDOXIN:NADP+ reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VW7
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: NAP, FDA, MG
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	309	28% helix, 28% strand	Q41736

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
FDA · Dihydroflavine-adenine dinucleotide · 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

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	418	0.65	0.78	44	NAP, FDA

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5VW7 · NADPH soak of Y316A mutant of corn root ferredoxin:NADP+ reductase · 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 5VW7 · PDBe 5VW7 · UniProt Q41736

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