› 5vmk

X-ray diffraction
2.55Å resolution

Crystal structure of a bifunctional GlmU UDP-N-acetylglucosamine diphosphorylase/glucosamine-1- phosphate N-acetyltransferase from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb5vmk/pdb
PDB entry 5vmk coloured by chain, front view.
PDB entry 5vmk coloured by chain, side view.
PDB entry 5vmk coloured by chain, top view.
Source organism: Acinetobacter baumannii
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109257 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 462 amino acids
Theoretical weight: 49.95 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: B0VPT6 (Residues: 1-454; Coverage: 100%)
Gene names: ABSDF3568, glmU
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CIT 3 x CIT
Ligand PO4 1 x PO4
Ligand PG4 3 x PG4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P3221
Unit cell:
a: 96.62Å b: 96.62Å c: 262.42Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.185 0.248
Expression system: Escherichia coli

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