1ta0

X-ray diffraction
2.1Å resolution

Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.

Released:
Source organism: Homo sapiens
Primary publication:
Structure and mechanism of RNA polymerase II CTD phosphatases.
Mol. Cell 15 399-407 (2004)
PMID: 15304220

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 22.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZU7 (Residues: 77-261; Coverage: 71%)
Gene names: CTDSP1, NIF3, NLIIF, SCP1
Sequence domains: NLI interacting factor-like phosphatase
Structure domains: HAD superfamily/HAD-like

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 117.82Å b: 47.17Å c: 40.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.227
Expression system: Escherichia coli