8q9p

X-ray diffraction
2.2Å resolution

Crystal Structure of the MADS-box/MEF2 Domain of MEF2D bound to dsDNA and HDAC5 deacetylase binding motif

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-270676 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
Histone deacetylase 5 Chain: X
Molecule details ›
Chain: X
Length: 18 amino acids
Theoretical weight: 2.08 KDa
Source organism: Homo sapiens
Expression system: synthetic construct
UniProt:
  • Canonical: Q9UQL6 (Residues: 179-195; Coverage: 2%)
Gene names: HDAC5, KIAA0600
MADS-box domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 95 amino acids
Theoretical weight: 11.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q05BX2 (Residues: 1-95; Coverage: 68%)
Gene name: MEF2D
Sequence domains: SRF-type transcription factor (DNA-binding and dimerisation domain)
MADS box dsDNA fw: AACTATTTATAAGA Chain: K
MADS box dsNA rev:TCTTATAAATAGTT Chain: L

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 54.243Å b: 56.748Å c: 76.689Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.262
Expression systems:
  • synthetic construct
  • Escherichia coli BL21(DE3)