› 2f46

X-ray diffraction
1.41Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase hydrolase-like protein phosphatase-like domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 156 amino acids
Theoretical weight: 17.91 KDa
Source organism: Neisseria meningitidis Z2491
Expression system: Escherichia coli
UniProt:
  • Canonical: A1KVD0 (Residues: 1-155; Coverage: 100%)
Gene name: NMC1647
Sequence domains: Beta-lactamase hydrolase-like protein, phosphatase-like domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand UNL 1 x UNL
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 144.278Å b: 33.466Å c: 59.899Å
α: 90° β: 96.18° γ: 90°
R-values:
R R work R free
0.201 0.2 0.228
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.
Böhmer et al. (2013)
2 more

3 mentions without citation

Using resonance synchronous spectroscopy to characterize the reactivity and electrophilicity of biologically relevant sulfane sulfur.
Li et al. (2019)
2 more