6wyn

X-ray diffraction
1.81Å resolution

Transition metal inhibition and structural refinement of the M. tuberculosis esterase, Rv0045c

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Esterase Rv0045c Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 35.59 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: I6XU97 (Residues: 2-298; Coverage: 100%)
Gene name: Rv0045c
Sequence domains: Alpha/beta hydrolase family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P3121
Unit cell:
a: 130.81Å b: 130.81Å c: 48.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.207 0.233
Expression system: Escherichia coli BL21