2pfr

X-ray diffraction
1.92Å resolution

Human N-acetyltransferase 2

Released:
Source organism: Homo sapiens
Entry authors: Tempel W, Wu H, Dombrovski L, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Grant DM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-145726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylamine N-acetyltransferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11245 (Residues: 2-290; Coverage: 100%)
Gene names: AAC2, NAT2
Sequence domains: N-acetyltransferase
Structure domains: Arylamine N-acetyltransferase fold

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E, null
Spacegroup: P43212
Unit cell:
a: 130.063Å b: 130.063Å c: 111.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.245
Expression system: Escherichia coli