› 5icw

X-ray diffraction
1.95Å resolution

Crystal structure of human NatF (hNaa60) homodimer bound to Coenzyme A

Released:
DOI: 10.2210/pdb5icw/pdb
PDB entry 5icw coloured by chain, front view.
PDB entry 5icw coloured by chain, side view.
PDB entry 5icw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation.
Støve SI, Magin RS, Foyn H, Haug BE, Marmorstein R, Arnesen T
Structure 24 1044-56 (2016)
PMID: 27320834

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + an N-terminal-L-methionyl-[transmembrane protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-[transmembrane protein] + CoA
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-alpha-acetyltransferase 60 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 182 amino acids
Theoretical weight: 20.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7X0 (Residues: 3-184; Coverage: 75%)
Gene names: HAT4, NAA60, NAT15, UNQ2771/PRO7155
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 4 x COA
1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 63.84Å b: 84.298Å c: 68.485Å
α: 90° β: 91.1° γ: 90°
R-values:
R R work R free
0.21 0.207 0.255
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Spotlight on protein N-terminal acetylation.
Ree et al. (2018)
2 more

5 mentions without citation

Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation.
Deng et al. (2021)
4 more