4nsq

X-ray diffraction
2.31Å resolution

Crystal structure of PCAF

Released:
Source organism: Homo sapiens
Primary publication:
Dimeric structure of p300/CBP associated factor.
OpenAccess logo BMC Struct. Biol. 14 2 (2014)
PMID: 24423233

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT2B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 190 amino acids
Theoretical weight: 21.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92831 (Residues: 493-658; Coverage: 20%)
Gene names: KAT2B, PCAF
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 4 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43
Unit cell:
a: 65.57Å b: 65.57Å c: 187.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.229 0.275
Expression system: Escherichia coli