Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129940 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Germinal-center associated nuclear protein
Molecule details ›
Chains: A, D
Length: 75 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Binding region of GANP to ENY2
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 75 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O60318 (Residues: 1163-1235; Coverage: 4%)
Sequence domains: Binding region of GANP to ENY2
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Transcription and mRNA export factor ENY2
Molecule details ›
Chains: B, C, E, F
Length: 101 amino acids
Theoretical weight: 11.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Transcription factor e(y)2
Structure domains: Serum Albumin; Chain A, Domain 1
Length: 101 amino acids
Theoretical weight: 11.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9NPA8 (Residues: 1-101; Coverage: 100%)
Sequence domains: Transcription factor e(y)2
Structure domains: Serum Albumin; Chain A, Domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU FR-E+ DW
Spacegroup:
P21
Expression system: Escherichia coli
