› 1knf

X-ray diffraction
1.9Å resolution

Crystal Structure of 2,3-dihydroxybiphenyl 1,2-dioxygenase Complexed with 3-methyl Catechol under Anaerobic Condition

Released:
DOI: 10.2210/pdb1knf/pdb
PDB entry 1knf coloured by chain, front view.
PDB entry 1knf coloured by chain, side view.
PDB entry 1knf coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol.
Vaillancourt FH, Han S, Fortin PD, Bolin JT, Eltis LD
J Biol Chem 273 34887-95 (1998)
PMID: 9857017

Function and Biology Details

Reaction catalysed: 
Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155618 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biphenyl-2,3-diol 1,2-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 32.38 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Burkholderia cepacia
UniProt:
  • Canonical: P47228 (Residues: 2-298; Coverage: 100%)
Gene names: Bxe_C1191, Bxeno_C1125, bphC
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

3 bound ligands:
Ligand FE2 2 x FE2
Ligand MBD 1 x MBD
Ligand TBU 2 x TBU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I422
Unit cell:
a: 123.1Å b: 123.1Å c: 110.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.168 0.195
Expression system: Burkholderia cepacia

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Citations

1 review citation

The ins and outs of ring-cleaving dioxygenases.
Vaillancourt et al. (2006)
45 other articles