› 4u9v

X-ray diffraction
1.78Å resolution

Crystal structure of NatD (Naa40p) bound to acetyl CoA

Released:
DOI: 10.2210/pdb4u9v/pdb
PDB 4u9v coloured by chain and viewed from the front.
PDB 4u9v coloured by chain and viewed from the side.
PDB 4u9v coloured by chain and viewed from the top.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (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

7 review citations

Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation.
Deng et al. (2021)
6 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