› 1cm0

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX

Released:
DOI: 10.2210/pdb1cm0/pdb
PDB entry 1cm0 coloured by chain, front view.
PDB entry 1cm0 coloured by chain, side view.
PDB entry 1cm0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.
Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R
EMBO J 18 3521-32 (1999)
PMID: 10393169

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187769 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT2B Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92831 (Residues: 491-658; Coverage: 20%)
Gene names: KAT2B, PCAF
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 2 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P64
Unit cell:
a: 97Å b: 97Å c: 77.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.223 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

23 review citations

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

11 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
10 more