5yge

X-ray diffraction
2.04Å resolution

ArgA complexed with AceCoA and glutamate

Released:
Model geometry
Fit model/data
Primary publication:
Crystal structure of l-glutamate N-acetyltransferase ArgA from Mycobacterium tuberculosis.
Biochim Biophys Acta Proteins Proteom 1865 1800-1807 (2017)
PMID: 28943401

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-128480 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino-acid acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 174 amino acids
Theoretical weight: 19.58 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O33289 (Residues: 2-174; Coverage: 99%)
Gene names: Rv2747, argA
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments


Cofactor: Ligand ACO 2 x ACO
2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P41212
Unit cell:
a: 73.728Å b: 73.728Å c: 187.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.197 0.221
Expression system: Escherichia coli BL21(DE3)