2ija

X-ray diffraction
1.7Å resolution

Human N-acetyltransferase 1 F125S mutant

Released:
Model geometry
Fit model/data
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
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148373 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylamine N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18440 (Residues: 2-290; Coverage: 100%)
Gene names: AAC1, NAT1
Sequence domains: N-acetyltransferase
Structure domains: Arylamine N-acetyltransferase fold

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 90.549Å b: 37.558Å c: 88.478Å
α: 90° β: 102.7° γ: 90°
R-values:
R R work R free
0.166 0.164 0.203
Expression system: Escherichia coli