› 2bv0

X-ray diffraction
1.8Å resolution

Crystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R133H in Complex with Protocatechuate.

Released:
DOI: 10.2210/pdb2bv0/pdb
PDB entry 2bv0 coloured by chain, front view.
PDB entry 2bv0 coloured by chain, side view.
PDB entry 2bv0 coloured by chain, top view.
Source organism: Acinetobacter baylyi ADP1
Primary publication:
Crystallographic Studies of Intradiol Dioxygenases.
Vetting MW
Phd Thesis (2001)

Function and Biology Details

Reaction catalysed: 
3,4-dihydroxybenzoate + O(2) = 3-carboxy-cis,cis-muconate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148968 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protocatechuate 3,4-dioxygenase alpha chain Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.49 KDa
Source organism: Acinetobacter baylyi ADP1
Expression system: Escherichia coli
UniProt:
  • Canonical: P20371 (Residues: 1-209; Coverage: 100%)
Gene names: ACIAD1712, pcaG
Sequence domains: Dioxygenase
Structure domains: Aromatic compound dioxygenase
Protocatechuate 3,4-dioxygenase beta chain Chain: B
Molecule details ›
Chain: B
Length: 241 amino acids
Theoretical weight: 27.58 KDa
Source organism: Acinetobacter baylyi ADP1
Expression system: Escherichia coli
UniProt:
  • Canonical: P20372 (Residues: 1-241; Coverage: 100%)
Gene names: ACIAD1711, pcaH
Sequence domains:
Structure domains: Aromatic compound dioxygenase

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand DHB 1 x DHB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: I23
Unit cell:
a: 144.95Å b: 144.95Å c: 144.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 0.192
Expression system: Escherichia coli

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