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Crystal structure of klebsiella pneumoniae udp-glucose 6-dehydrogenase complexed with NADH and udp-glucose

Analyse Crystal structure of klebsiella pneumoniae udp-glucose 6-dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PLR
Type: protein
Length: 377 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: NAI, U5P
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-glucose 6-dehydrogenase (EC 1.1.1.22)	protein	377	46% helix, 15% strand	C4XAX5

Ligands and binding sites

NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
U5P · Uridine-5'-monophosphate · ligand · 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	623	0.68	0.77	68	NAI, U5P
2	107	0.37	0.74	18	empty

Compared structures

3PLR · Crystal structure of Klebsiella pneumoniae UDP-glucose 6-dehydrogenase 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 3PLR · PDBe 3PLR · UniProt C4XAX5

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