1knf Summary


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

The structure was published by Vaillancourt, F.H., Han, S., Fortin, P.D., Bolin, J.T., and Eltis, L.D., in 1998 in a paper entitled "Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2001.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE. This molecule has the UniProt identifier P47228 (BPHC_BURXL)search. The sample contained 297 residues which is 100% of the natural sequence. Out of 297 residues 288 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homooctamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE P47228 (2-298) (BPHC_BURXL)search Burkholderia xenovorans LB400search 100% 297 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P47228 (2 - 298) 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE Burkholderia xenovorans LB400

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P47228) Extradiol dioxygenasessearch 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1search PF00903: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamilysearch

Chain ID Biological process (GO) Molecular function (GO)
A (P47228) xenobiotic catabolic processsearch oxidation-reduction processsearch cellular aromatic compound metabolic processsearch aromatic compound catabolic processsearch biphenyl-2,3-diol 1,2-dioxygenase activitysearch dioxygenase activitysearch ferrous iron bindingsearch iron ion bindingsearch catalytic activitysearch metal ion bindingsearch oxidoreductase activitysearch

Chain InterPro annotation
A Extradiol ring-cleavage dioxygenase, class I /IIsearch Glyoxalase/fosfomycin resistance/dioxygenase domainsearch 2,3-dihydroxybiphenyl 1,2-dioxygenasesearch Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenasesearch