We've built a new version of this page with an interactive 3D viewer. Try it out in beta and help us improve:

› 1nzy

X-ray diffraction
1.8Å resolution

4-CHLOROBENZOYL COENZYME A DEHALOGENASE FROM PSEUDOMONAS SP. STRAIN CBS-3

Released:
DOI: 10.2210/pdb1nzy/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1nzy coloured by chain, front view.
PDB entry 1nzy coloured by chain, side view.
PDB entry 1nzy coloured by chain, top view.
Source organism: Pseudomonas sp. CBS3
Primary publication:
Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 A resolution: an enzyme catalyst generated via adaptive mutation.
Benning MM, Taylor KL, Yang G, Xiang H, Wesenberg G, Dunaway-Mariano D, Holden HM
Biochemistry 35 8103-9 (1996)
PMID: 8679561

Function and Biology Details

Reaction catalysed: 
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride + H(+).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero hexamer
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107644 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
4-chlorobenzoyl coenzyme A dehalogenase Chains: A, C
Molecule details ›
Chains: A, C
Length: 269 amino acids
Theoretical weight: 29.9 KDa
Source organism: Pseudomonas sp. CBS3
Expression system: Escherichia coli
UniProt:
  • Canonical: A5JTM5 (Residues: 1-269; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:
4-chlorobenzoyl coenzyme A dehalogenase Chain: B
Molecule details ›
Chain: B
Length: 269 amino acids
Theoretical weight: 29.9 KDa
Source organism: Pseudomonas sp. CBS3
Expression system: Escherichia coli
UniProt:
  • Canonical: A5JTM5 (Residues: 1-269; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments


Cofactor: Ligand BCA 3 x BCA
3 bound ligands:
Ligand CA 3 x CA
Ligand PO4 1 x PO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P21212
Unit cell:
a: 107.8Å b: 102.4Å c: 90.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
15 more

8 mentions without citation

Using sequence similarity networks for visualization of relationships across diverse protein superfamilies.
Atkinson et al. (2009)
7 more