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Crystal structure of ferredoxin reductase, BPHA4 (oxidized form)

Analyse Crystal structure of ferredoxin reductase, BPHA4 (oxidized form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GQW
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin reductase
EC: 1.18.1.2
Ligands: FAD
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin reductase (EC 1.18.1.2)	protein	401	27% helix, 30% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
FMT · Formic acid · additive · 5 copies · chains A
GOL · Glycerol · 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	825	0.83	0.85	93	FAD, GOL

Compared structures

2GQW · Crystal structure of Ferredoxin reductase, BphA4 (oxidized form) · 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
Elsewhere: RCSB PDB 2GQW · PDBe 2GQW

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