4hny

X-ray diffraction
2.25Å resolution

Apo N-terminal acetyltransferase complex A

Released:
Model geometry
Fit model/data
Entry authors: Neubauer JL, Immormino RM, Dollins DE, Endo-Streeter ST, Pemble IV CW, York JD

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-139531 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-terminal acetyltransferase A complex subunit NAT1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 863 amino acids
Theoretical weight: 100.13 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P12945 (Residues: 1-854; Coverage: 100%)
Gene names: AAA1, D2720, NAT1, YDL040C
Sequence domains: N-terminal acetyltransferase A, auxiliary subunit
N-terminal acetyltransferase A complex catalytic subunit ARD1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 248 amino acids
Theoretical weight: 28.82 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P07347 (Residues: 1-238; Coverage: 100%)
Gene names: ARD1, YHR013C
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P31
Unit cell:
a: 129.416Å b: 129.416Å c: 171.783Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.178 0.22
Expression system: Escherichia coli