› 1su1

X-ray diffraction
2.25Å resolution

Structural and biochemical characterization of Yfce, a phosphoesterase from E. coli

Released:
DOI: 10.2210/pdb1su1/pdb
PDB entry 1su1 coloured by chain, front view.
PDB entry 1su1 coloured by chain, side view.
PDB entry 1su1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.
Miller DJ, Shuvalova L, Evdokimova E, Savchenko A, Yakunin AF, Anderson WF
Protein Sci 16 1338-48 (2007)
PMID: 17586769

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphodiesterase YfcE Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 208 amino acids
Theoretical weight: 22.91 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P67095 (Residues: 1-184; Coverage: 100%)
Gene names: JW5377, b2300, yfcE
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P31
Unit cell:
a: 71.02Å b: 71.02Å c: 173.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.213 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Metallophosphoesterases: structural fidelity with functional promiscuity.
Matange et al. (2015)
12 other articles

6 mentions without citation

From complete genome sequence to 'complete' understanding?
Galperin et al. (2010)
5 more