› 5j8c

X-ray diffraction
2.17Å resolution

Human MOF C316S, E350Q crystal structure

Released:
DOI: 10.2210/pdb5j8c/pdb
PDB entry 5j8c coloured by chain, front view.
PDB entry 5j8c coloured by chain, side view.
PDB entry 5j8c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation.
McCullough CE, Song S, Shin MH, Johnson FB, Marmorstein R
J Biol Chem 291 18190-8 (2016)
PMID: 27382063

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT8 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 36.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H7Z6 (Residues: 177-458; Coverage: 62%)
Gene names: KAT8, MOF, MYST1, PP7073
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand CL 2 x CL
Ligand NA 2 x NA
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 46.148Å b: 55.676Å c: 122.311Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.19 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
3 more

1 mention without citation

Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation.
McCullough et al. (2016)