› 1dmh

X-ray diffraction
1.7Å resolution

STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 WITH BOUND 4-METHYLCATECHOL

Released:
DOI: 10.2210/pdb1dmh/pdb
PDB entry 1dmh coloured by chain, front view.
PDB entry 1dmh coloured by chain, side view.
PDB entry 1dmh coloured by chain, top view.
Source organism: Acinetobacter baylyi ADP1
Primary publication:
The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Vetting MW, Ohlendorf DH
Structure 8 429-40 (2000)
PMID: 10801478

Function and Biology Details

Reaction catalysed: 
Catechol + O(2) = cis,cis-muconate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139755 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol 1,2-dioxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 311 amino acids
Theoretical weight: 34.38 KDa
Source organism: Acinetobacter baylyi ADP1
Expression system: Escherichia coli
UniProt:
  • Canonical: P07773 (Residues: 1-311; Coverage: 100%)
Gene names: ACIAD1442, catA
Sequence domains:
Structure domains: Aromatic compound dioxygenase

Ligands and Environments

3 bound ligands:
Ligand FE 2 x FE
Ligand MCT 2 x MCT
Ligand LIO 2 x LIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 52.8Å b: 88Å c: 84.4Å
α: 90° β: 96.3° γ: 90°
R-values:
R R work R free
0.185 0.185 0.218
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The ins and outs of ring-cleaving dioxygenases.
Vaillancourt et al. (2006)
7 more

3 mentions without citation

Alternate splicing of dysferlin C2A confers Ca²⁺-dependent and Ca²⁺-independent binding for membrane repair.
Fuson et al. (2014)
2 more