› 1lgt

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE (DHBD) COMPLEXED WITH 2'-Cl DIHYDROXYBIPHENYL (DHB)

Released:
DOI: 10.2210/pdb1lgt/pdb
PDB entry 1lgt coloured by chain, front view.
PDB entry 1lgt coloured by chain, side view.
PDB entry 1lgt coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
Identification and analysis of a bottleneck in PCB biodegradation.
Dai S, Vaillancourt FH, Maaroufi H, Drouin NM, Neau DB, Snieckus V, Bolin JT, Eltis LD
Nat Struct Biol 9 934-9 (2002)
PMID: 12415290

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: Pseudomonas putida
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

2 bound ligands:
Ligand FE2 2 x FE2
Ligand BP3 2 x BP3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I422
Unit cell:
a: 122.337Å b: 122.337Å c: 106.947Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.236
Expression system: Pseudomonas putida

Quick links

Citations

9 review citations

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