4qqg

X-ray diffraction
2.8Å resolution

Crystal structure of an N-terminal HTATIP fragment

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-187828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT5 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 81 amino acids
Theoretical weight: 9.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92993 (Residues: 1-80; Coverage: 16%)
Gene names: HTATIP, KAT5, TIP60
Sequence domains: RNA binding activity-knot of a chromodomain
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 43.544Å b: 59.986Å c: 101.638Å
α: 90° β: 100.65° γ: 90°
R-values:
R R work R free
0.228 0.226 0.26
Expression system: Escherichia coli BL21(DE3)