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Structure paper

TitleThe Lid Domain of the MCP Hydrolase DxnB2 Contributes to the Reactivity toward Recalcitrant PCB Metabolites.
Journal, issue, pagesBiochemistry, Vol. 52, Page 5685-5695, Year 2013
Publish dateJul 29, 2013 (structure data deposition date)
AuthorsRuzzini, A.C. / Bhowmik, S. / Yam, K.C. / Ghosh, S. / Bolin, J.T. / Eltis, L.D.
External linksBiochemistry / PubMed:23879719
MethodsX-ray diffraction
Resolution2.02 - 2.26 Å
Structure data

PDB-4lxg:
Crystal structure of DxnB2, a carbon - carbon bond hydrolase from Sphingomonas wittichii RW1
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-4lxh:
Crystal Structure of the S105A mutant of a carbon-carbon bond hydrolase, DxnB2 from Sphingomonas wittichii RW1, in complex with 3-Cl HOPDA
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-4lyd:
Crystal structure of the S105A mutant of a C-C hydrolase, DxnB2 from Sphingomonas wittichii RW1
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-C1E:
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid

ChemComp-NA:
Unknown entry

Source
  • sphingomonas wittichii rw1 (bacteria)
  • sphingomonas wittichii (bacteria)
KeywordsHYDROLASE / Carbon-carbon bond hydrolase / Rossmann Fold / alpha/beta hydrolase fold / Cytosolic / meta-cleavage product hydrolase / C-C bond hydrolase / alpha-beta hydrolase / dibenzo-p-dioxin degradation / dibenzofuran degradation

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