› 4nsq

X-ray diffraction
2.31Å resolution

Crystal structure of PCAF

Released:
DOI: 10.2210/pdb4nsq/pdb
PDB entry 4nsq coloured by chain, front view.
PDB entry 4nsq coloured by chain, side view.
PDB entry 4nsq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dimeric structure of p300/CBP associated factor.
Shi S, Lin J, Cai Y, Yu J, Hong H, Ji K, Downey JS, Lu X, Chen R, Han J, Han A
BMC Struct Biol 14 2 (2014)
PMID: 24423233

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187770 (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

Quick links

Citations

1 review citation

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
5 other articles

6 mentions without citation

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