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Crystal structure of NADP bound GDP-L-fucose synthase from brucella ovis

Analyse Crystal structure of NADP bound GDP-L-fucose synthase from brucella ovis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8DU0
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GDP-L-fucose synthase
EC: 1.1.1.271
UniProt: A0A0H3AU93
Ligands: NAP
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GDP-L-fucose synthase (EC 1.1.1.271)	protein	286	49% helix, 13% strand	A0A0H3AU93

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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	672	0.71	0.78	67	NAP

Compared structures

8DU0 · Crystal Structure of NADP bound GDP-L-fucose synthase from Brucella ovis · 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 A0A0H3AU93
Elsewhere: RCSB PDB 8DU0 · PDBe 8DU0 · UniProt A0A0H3AU93

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