› 6iht

X-ray diffraction
1.57Å resolution

Crystal structure of bacterial serine phosphatase bound with phosphorylated peptide

Released:
DOI: 10.2210/pdb6iht/pdb
PDB entry 6iht coloured by chain, front view.
PDB entry 6iht coloured by chain, side view.
PDB entry 6iht coloured by chain, top view.
Source organisms:
Primary publication:
Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase.
Yang T, Liu T, Gan J, Yu K, Chen K, Xue W, Lan L, Yang S, Yang CG
ACS Infect Dis 5 841-850 (2019)
PMID: 30868877

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166890 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
protein-serine/threonine phosphatase Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.14 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RL81 (Residues: 3-247; Coverage: 99%)
Gene names: A6760_05000, BN1321_240063, EP54_08495, EQ90_08165, FAF17_11265, GO793_10355, GO814_06360, GO942_07250, NCTC10702_01924, NCTC13131_00423, NCTC7972_00731, SAMEA1531725_01588, SAMEA2078260_01528, SAMEA2078588_01607, SAMEA2080344_01697, SAMEA2081063_01376, SAMEA4008575_01865, SAMEA70146418_01691, SAMEA70245418_01977, prpC, prpC_1
Sequence domains: Protein phosphatase 2C
His12 Chain: X
Molecule details ›
Chain: X
Length: 3 amino acids
Theoretical weight: 299 Da
Source organism: Peptide display vector fth1
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand MN 4 x MN
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P21
Unit cell:
a: 46.693Å b: 38.609Å c: 65.003Å
α: 90° β: 101.89° γ: 90°
R-values:
R R work R free
0.16 0.159 0.183
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 citation in other articles

Insight into the Dual Inhibition Mechanism of Corilagin against MRSA Serine/Threonine Phosphatase (Stp1) by Molecular Modeling.
Yang et al. (2020)
1 more