› 4ygy

X-ray diffraction
2.36Å resolution

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

Released:
DOI: 10.2210/pdb4ygy/pdb
PDB entry 4ygy coloured by chain, front view.
PDB entry 4ygy coloured by chain, side view.
PDB entry 4ygy coloured by chain, top view.
Source organisms:
Primary publication:
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
Mayfield JE, Fan S, Wei S, Zhang M, Li B, Ellington AD, Etzkorn FA, Zhang YJ
ACS Chem Biol 10 2405-14 (2015)
PMID: 26332362

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165375 (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
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
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:
Ligand MG 2 x MG
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-values:
R R work R free
0.186 0.183 0.246
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.
Zhou et al. (2016)
3 more

3 mentions without citation

Targeting the C-Terminal Domain Small Phosphatase 1.
Rallabandi et al. (2020)
2 more