› 1bob

X-ray diffraction
2.3Å resolution

HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A

Released:
DOI: 10.2210/pdb1bob/pdb
PDB entry 1bob coloured by chain, front view.
PDB entry 1bob coloured by chain, side view.
PDB entry 1bob coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V
Cell 94 427-38 (1998)
PMID: 9727486

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase type B catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 37.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12341 (Residues: 1-320; Coverage: 86%)
Gene names: HAT1, LPA16W, YP8132.12, YPL001W
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 111.3Å b: 47.9Å c: 75.7Å
α: 90° β: 90.3° γ: 90°
R-values:
R R work R free
0.204 0.204 0.269
Expression system: Escherichia coli

Quick links

Citations

37 review citations

Histone acetyltransferases.
Roth et al. (2001)
36 more

18 mentions without citation

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