› 3qah

X-ray diffraction
2.1Å resolution

Crystal structure of apo-form human MOF catalytic domain

Released:
DOI: 10.2210/pdb3qah/pdb
PDB entry 3qah coloured by chain, front view.
PDB entry 3qah coloured by chain, side view.
PDB entry 3qah coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274.
Sun B, Guo S, Tang Q, Li C, Zeng R, Xiong Z, Zhong C, Ding J
Cell Res 21 1262-6 (2011)
PMID: 21691301

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: 304 amino acids
Theoretical weight: 35.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7Z6 (Residues: 174-449; Coverage: 60%)
Gene names: KAT8, MOF, MYST1, PP7073
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 45.913Å b: 60.69Å c: 124.368Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.228
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Writers and readers of histone acetylation: structure, mechanism, and inhibition.
Marmorstein et al. (2014)
10 more

4 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
3 more