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Crystal structure of udp-glucose 4-epimerase from brucella ovis in complex with NAD

Analyse Crystal structure of udp-glucose 4-epimerase from brucella ovis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WOK
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucose 4-epimerase
EC: 5.1.3.2
UniProt: A5VUK4
Ligands: NAD, ZN, PO4
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose 4-epimerase (EC 5.1.3.2)	protein	325	41% helix, 17% strand	A5VUK4

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 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	887	0.81	0.83	72	NAD

Compared structures

4WOK · Crystal structure of UDP-glucose 4-epimerase from Brucella ovis in complex with NAD · 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 A5VUK4
Elsewhere: RCSB PDB 4WOK · PDBe 4WOK · UniProt A5VUK4

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