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Crystal structure of udp-N-acetylenolpyruvylglucosamine reductase (murb) from thermus caldophilus

Analyse Crystal structure of udp-N-acetylenolpyruvylglucosamine reductase (murb) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GQU
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylenolpyruvylglucosamine reductase
EC: 1.1.1.158
Ligands: FAD, EPU
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylenolpyruvylglucosamine reductase (EC 1.1.1.158)	protein	266	29% helix, 29% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
EPU · Uridine-diphosphate-2(N-acetylglucosaminyl) butyric acid · ligand · 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	710	0.77	0.82	81	FAD, EPU

Compared structures

2GQU · Crystal Structure of UDP-N-Acetylenolpyruvylglucosamine Reductase (MurB) from Thermus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2GQU · PDBe 2GQU

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