7d0p

X-ray diffraction
1.8Å resolution

Crystal structure of human HBO1-BRPF2 in complex with propionyl-coenzyme A

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
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: 32.6 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
UniProt:
  • Canonical: O95696 (Residues: 31-80; Coverage: 5%)
Gene names: BRD1, BRL, BRPF2

Ligands and Environments


Cofactor: Ligand 1VU 1 x 1VU
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2
Unit cell:
a: 126.679Å b: 39.306Å c: 87.744Å
α: 90° β: 123.01° γ: 90°
R-values:
R R work R free
0.173 0.171 0.226
Expression system: Escherichia coli