2fbm

X-ray diffraction
2.28Å resolution

Acetyltransferase domain of CDY1

Released:
Source organism: Homo sapiens
Entry authors: Min JR, Antoshenko T, Hong W, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)

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:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-195361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Testis-specific chromodomain protein Y 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 291 amino acids
Theoretical weight: 32.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6F8 (Residues: 281-531; Coverage: 47%)
Gene names: CDY1, CDY1A, CDY1B
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 115.925Å b: 133.767Å c: 122.629Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.187 0.253
Expression system: Escherichia coli