2buq

X-ray diffraction
1.8Å resolution

Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with Catechol

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 24-mer (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: 23.51 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: I23
Unit cell:
a: 144.7Å b: 144.7Å c: 144.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.165 0.194
Expression system: Escherichia coli