› 6wyn

X-ray diffraction
1.81Å resolution

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

Released:
DOI: 10.2210/pdb6wyn/pdb
PDB entry 6wyn coloured by chain, front view.
PDB entry 6wyn coloured by chain, side view.
PDB entry 6wyn coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.
Bowles IE, Pool EH, Lancaster BS, Lawson EK, Savas CP, Kartje ZJ, Severinac L, Cho DH, Macbeth MR, Johnson RJ, Hoops GC
Protein Sci 30 1554-1565 (2021)
PMID: 33914998

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125192 (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:
Ligand CL 1 x CL
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

Quick links

Citations

2 citation in other articles

Revisiting Jatropha curcas Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model.
Schwarz et al. (2021)
1 more

1 mention without citation

Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.
Bowles et al. (2021)