1o12

X-ray diffraction
2.5Å resolution

Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution

Released:
Source organism: Thermotoga maritima
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
N-acetyl-D-glucosamine 6-phosphate + H(2)O = D-glucosamine 6-phosphate + acetate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-194631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidohydrolase-related domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 376 amino acids
Theoretical weight: 42.19 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZS1 (Residues: 1-364; Coverage: 100%)
Gene name: TM_0814
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P3121
Unit cell:
a: 85.07Å b: 85.07Å c: 206.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.251
Expression system: Escherichia coli