› 4ua3

X-ray diffraction
1.85Å resolution

Crystal structure of selenomethionine labeled SpNatD

Released:
DOI: 10.2210/pdb4ua3/pdb
PDB entry 4ua3 coloured by chain, front view.
PDB entry 4ua3 coloured by chain, side view.
PDB entry 4ua3 coloured by chain, top view.
Source organism: Schizosaccharomyces pombe 972h-
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:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-alpha-acetyltransferase 40 Chains: A, B
Molecule details ›
Chains: A, B
Length: 194 amino acids
Theoretical weight: 23.34 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9USH6 (Residues: 13-204; Coverage: 94%)
Gene names: SPCC825.04c, naa40
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 2 x COA
1 bound ligand:
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 114.701Å b: 42.629Å c: 85.417Å
α: 90° β: 98.68° γ: 90°
R-values:
R R work R free
0.182 0.179 0.239
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

4 mentions without citation

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