4v2i

X-ray diffraction
1.69Å resolution

Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium Thalassospira sp

Released:

Function and Biology Details

Reaction catalysed:
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-100054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 34.96 KDa
Source organism: Thalassospira sp. GB04J01
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A023T3X2 (Residues: 28-343; Coverage: 100%)
Gene name: Est2349
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 73.326Å b: 85.429Å c: 91.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.182
Expression system: Escherichia coli BL21(DE3)