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X-ray structure of the ferredoxin-NADP reductase from brucella ovis in complex with NADP

Analyse X-ray structure of the ferredoxin-NADP reductase from brucella ovis in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RRA
Type: protein
Length: 257 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: A0A0H3ASL8
Ligands: FAD, NAP, SO4
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	257	27% helix, 33% strand	A0A0H3ASL8

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
SO4 · Sulfate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	489	0.68	0.79	45	FAD, NAP
2	130	0.40	0.74	28	empty

Compared structures

6RRA · X-ray structure of the ferredoxin-NADP reductase from brucella ovis in complex with NADP · 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 A0A0H3ASL8
Elsewhere: RCSB PDB 6RRA · PDBe 6RRA · UniProt A0A0H3ASL8

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