› 2l9s

Solution NMR

Solution structure of Pf1 SID1-mSin3A PAH2 Complex

Released:
DOI: 10.2210/pdb2l9s/pdb
PDB entry 2l9s coloured by chain, ensemble of 20 models, front view.
PDB entry 2l9s coloured by chain, ensemble of 20 models, side view.
PDB entry 2l9s coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.
Kumar GS, Xie T, Zhang Y, Radhakrishnan I
J Mol Biol 408 987-1000 (2011)
PMID: 21440557

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178789 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PHD finger protein 12 Chain: A
Molecule details ›
Chain: A
Length: 45 amino acids
Theoretical weight: 4.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96QT6 (Residues: 200-241; Coverage: 4%)
Gene names: KIAA1523, PHF12
Sequence domains: PHD finger protein 12 MRG binding domain
Structure domains: PHD finger protein 12
Paired amphipathic helix protein Sin3a Chain: B
Molecule details ›
Chain: B
Length: 94 amino acids
Theoretical weight: 10.82 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60520 (Residues: 295-385; Coverage: 7%)
Gene names: Kiaa4126, Sin3a
Sequence domains: Paired amphipathic helix repeat
Structure domains: Paired amphipathic helix

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 81%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Co-repressor, co-activator and general transcription factor: the many faces of the Sin3 histone deacetylase (HDAC) complex.
Adams et al. (2018)
2 more

2 mentions without citation

Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.
Kumar et al. (2011)
1 more