3msr

X-ray diffraction
2.16Å resolution

The crystal structure of an amidohydrolase from Mycoplasma synoviae

Released:
Source organism: Mycoplasmopsis synoviae 53
Entry authors: Zhang Z, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reactions catalysed:
D-xylono-1,4-lactone 5-phosphate + H(2)O = 5-phospho-D-xylonate
A 1,4-lactone + H(2)O = a 4-hydroxyacid
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
homo dimer
PDBe Complex ID:
PDB-CPX-175431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospho-furanose lactonase Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 41.1 KDa
Source organism: Mycoplasmopsis synoviae 53
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4A724 (Residues: 2-353; Coverage: 100%)
Gene name: MS53_0025
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6322
Unit cell:
a: 111.248Å b: 111.248Å c: 138.308Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 0.15 0.192
Expression system: Escherichia coli BL21(DE3)