› 4u9v

X-ray diffraction
1.78Å resolution

Crystal structure of NatD (Naa40p) bound to acetyl CoA

Released:
DOI: 10.2210/pdb4u9v/pdb
PDB entry 4u9v coloured by chain, front view.
PDB entry 4u9v coloured by chain, side view.
PDB entry 4u9v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.
Magin RS, Liszczak GP, Marmorstein R
Structure 23 332-41 (2015)
PMID: 25619998

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-N(alpha)-acetyl-L-seryl-[histone H2A] + CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-alpha-acetyltransferase 40 Chain: B
Molecule details ›
Chain: B
Length: 197 amino acids
Theoretical weight: 22.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86UY6 (Residues: 25-220; Coverage: 83%)
Gene names: NAA40, NAT11, PATT1
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 88.256Å b: 44.064Å c: 50.356Å
α: 90° β: 95.44° γ: 90°
R-values:
R R work R free
0.169 0.167 0.206
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

5 mentions without citation

The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.
Magin et al. (2015)
4 more