› 3i2f

X-ray diffraction
2.5Å resolution

Cocaine Esterase with mutations T172R / G173Q, bound to DTT adduct

Released:
DOI: 10.2210/pdb3i2f/pdb
PDB entry 3i2f coloured by chain, front view.
PDB entry 3i2f coloured by chain, side view.
PDB entry 3i2f coloured by chain, top view.
Source organism: Rhodococcus sp. MB1 'Bresler 1999'
Primary publication:
Structural analysis of thermostabilizing mutations of cocaine esterase.
Narasimhan D, Nance MR, Gao D, Ko MC, Macdonald J, Tamburi P, Yoon D, Landry DM, Woods JH, Zhan CG, Tesmer JJ, Sunahara RK
Protein Eng Des Sel 23 537-47 (2010)
PMID: 20436035

Function and Biology Details

Reaction catalysed: 
Cocaine + H(2)O = ecgonine methyl ester + benzoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cocaine esterase Chain: A
Molecule details ›
Chain: A
Length: 587 amino acids
Theoretical weight: 63.84 KDa
Source organism: Rhodococcus sp. MB1 'Bresler 1999'
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L9D7 (Residues: 1-574; Coverage: 100%)
Gene name: cocE
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CL 8 x CL
Ligand DBC 1 x DBC
Ligand GOL 3 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P6522
Unit cell:
a: 106.25Å b: 106.25Å c: 220.041Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.173 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Accelerating cocaine metabolism as an approach to the treatment of cocaine abuse and toxicity.
Schindler et al. (2012)
2 more

5 mentions without citation

Structural analysis of thermostabilizing mutations of cocaine esterase.
Narasimhan et al. (2010)
4 more