X-ray diffraction
2.36Å resolution

Crystal Structure of Human Scp1 bound to trans-proline peptidomimetic CTD phospho-Ser5 peptide


Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 21.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • 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
peptidomimetic CTD phospho-Ser5 peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.26 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 125.28Å b: 78.335Å c: 63.031Å
α: 90° β: 112.59° γ: 90°
R R work R free
0.186 0.183 0.246
Expression systems:
  • Escherichia coli
  • Not provided