› 2hm7

X-ray diffraction
2Å resolution

Crystal Structure Analysis of the G84S EST2 mutant

Released:
DOI: 10.2210/pdb2hm7/pdb
PDB entry 2hm7 coloured by chain, front view.
PDB entry 2hm7 coloured by chain, side view.
PDB entry 2hm7 coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius
Primary publication:
Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius.
Mandrich L, Menchise V, Alterio V, De Simone G, Pedone C, Rossi M, Manco G
Proteins 71 1721-31 (2008)
PMID: 18076040

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
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-181976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 34.37 KDa
Source organism: Alicyclobacillus acidocaldarius
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7SIG1 (Residues: 1-310; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 63.66Å b: 82.17Å c: 47.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 citation in other articles

The functional G143E variant of carboxylesterase 1 is associated with increased clopidogrel active metabolite levels and greater clopidogrel response.
Lewis et al. (2013)
14 more

3 mentions without citation

Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.
Ohara et al. (2014)
2 more