5n9m

X-ray diffraction
1.85Å resolution

Crystal structure of GatD - a glutamine amidotransferase from Staphylococcus aureus involved in peptidoglycan amidation

Released:

Function and Biology Details

Reactions catalysed:
L-glutamine + H(2)O = L-glutamate + NH(3)
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-101624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 27.47 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2WZ38 (Residues: 1-243; Coverage: 100%)
Gene names: SACOL1950, gatD
Sequence domains: CobB/CobQ-like glutamine amidotransferase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 48.61Å b: 93.92Å c: 110.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.186
Expression system: Escherichia coli