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Crystal structure of udp-glucose dehydrogenase from klebsiella pneumoniae complexed with product udp-glucuronic acid

Analyse Crystal structure of udp-glucose dehydrogenase from klebsiella pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PJG
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-glucose 6-dehydrogenase
EC: 1.1.1.22
UniProt: C4XAX5
Ligands: UGA
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose 6-dehydrogenase (EC 1.1.1.22)	protein	389	43% helix, 14% strand	C4XAX5

Ligands and binding sites

UGA · Uridine-5'-diphosphate-glucuronic acid · ligand · 2 copies · chains A
CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 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	1114	0.80	0.81	102	UGA
2	87	0.42	0.79	15	empty

Compared structures

3PJG · Crystal structure of UDP-glucose dehydrogenase from Klebsiella pneumoniae complexed with… · 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 C4XAX5
Elsewhere: RCSB PDB 3PJG · PDBe 3PJG · UniProt C4XAX5

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