Function and Biology Details
Reaction catalysed:
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114652 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
Myocyte-specific enhancer factor 2B
Molecule details ›
Chains: P, Q, R, S
Length: 93 amino acids
Theoretical weight: 11.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: SRF-type transcription factor (DNA-binding and dimerisation domain)
Structure domains: Transcription factor, MADS-box
Length: 93 amino acids
Theoretical weight: 11.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q02080 (Residues: 1-93; Coverage: 26%)
Sequence domains: SRF-type transcription factor (DNA-binding and dimerisation domain)
Structure domains: Transcription factor, MADS-box
Histone deacetylase 9
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU
Spacegroup:
P1
Expression system: Escherichia coli
