2fw2

X-ray diffraction
2.2Å resolution

Catalytic domain of CDY

Released:
Source organism: Homo sapiens
Entry authors: Min JR, Antoshenko T, Wu H, Weigelt J, Sundstrom M, Arrowsmith C, 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

Assemblies composition:
homo hexamer
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-195359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Testis-specific chromodomain protein Y 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 260 amino acids
Theoretical weight: 28.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6F7 (Residues: 282-541; Coverage: 48%)
Gene names: CDY2, CDY2A, CDY2B
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 80.454Å b: 133.579Å c: 82.328Å
α: 90° β: 117.56° γ: 90°
R-values:
R R work R free
0.188 0.185 0.253
Expression system: Escherichia coli