2huz

X-ray diffraction
2.67Å resolution

Crystal structure of GNPNAT1

Released:
Source organism: Homo sapiens
Entry authors: Min J, Wu H, Zeng H, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine 6-phosphate N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 20.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96EK6 (Residues: 1-184; Coverage: 100%)
Gene names: GNA1, GNPNAT1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 111.668Å b: 47.645Å c: 84.843Å
α: 90° β: 123.52° γ: 90°
R-values:
R R work R free
0.205 0.2 0.298
Expression system: Escherichia coli