4imi

X-ray diffraction
2.35Å resolution

Novel Modifications on C-terminal Domain of RNA Polymerase II can Fine- tune the Phosphatase Activity of Ssu72.

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate

Structure analysis Details

Assemblies composition:
hetero dimer
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-164580 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Symplekin Chains: A, C
Molecule details ›
Chains: A, C
Length: 339 amino acids
Theoretical weight: 37.5 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8MSU4 (Residues: 19-351; Coverage: 29%)
Gene names: CG2097, Sym
Sequence domains: Symplekin/PTA1 N-terminal
Structure domains: Leucine-rich Repeat Variant
RNA polymerase II subunit A C-terminal domain phosphatase SSU72 Chains: B, D
Molecule details ›
Chains: B, D
Length: 200 amino acids
Theoretical weight: 23.13 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9VWE4 (Residues: 1-195; Coverage: 100%)
Gene names: BEST:CK01830, CG14216, Dmel\CG14216, Dmel_CG14216, Ssu72, dSsu72
Sequence domains: Ssu72-like protein
Structure domains:
CTD Chain: F

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P4
Unit cell:
a: 128.335Å b: 128.335Å c: 106.112Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.219 0.239
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided