› 5gk9

X-ray diffraction
2.4Å resolution

Crystal structure of human HBO1 in complex with BRPF2

Released:
DOI: 10.2210/pdb5gk9/pdb
PDB entry 5gk9 coloured by chain, front view.
PDB entry 5gk9 coloured by chain, side view.
PDB entry 5gk9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.
Tao Y, Zhong C, Zhu J, Xu S, Ding J
Nucleic Acids Res 45 5707-5719 (2017)
PMID: 28334966

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131866 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase KAT7 Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 32.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95251 (Residues: 336-611; Coverage: 45%)
Gene names: HBO1, HBOa, KAT7, MYST2
Sequence domains:
Bromodomain-containing protein 1 Chain: B
Molecule details ›
Chain: B
Length: 50 amino acids
Theoretical weight: 5.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O95696 (Residues: 31-80; Coverage: 5%)
Gene names: BRD1, BRL, BRPF2

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 126.47Å b: 39.321Å c: 87.666Å
α: 90° β: 122.1° γ: 90°
R-values:
R R work R free
0.26 0.233 0.26
Expression systems:
  • Escherichia coli
  • Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

3 review citations

Deciphering structure, function and mechanism of lysine acetyltransferase HBO1 in protein acetylation, transcription regulation, DNA replication and its oncogenic properties in cancer.
Lan et al. (2020)
2 more

6 mentions without citation

Molecular basis for chromatin assembly and modification by multiprotein complexes.
Ricketts et al. (2019)
5 more