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Structure paper

TitleEvolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Journal, issue, pagesBiochemistry, Vol. 39, Page 4590-4602, Year 2000
Publish dateJan 25, 2000 (structure data deposition date)
AuthorsGulick, A.M. / Hubbard, B.K. / Gerlt, J.A. / Rayment, I.
External linksBiochemistry / PubMed:10769114
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-1ec7:
E. COLI GLUCARATE DEHYDRATASE NATIVE ENZYME
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1ec8:
E. COLI GLUCARATE DEHYDRATASE BOUND TO PRODUCT 2,3-DIHYDROXY-5-OXO-HEXANEDIOATE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1ec9:
E. COLI GLUCARATE DEHYDRATASE BOUND TO XYLAROHYDROXAMATE
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1ecq:
E. COLI GLUCARATE DEHYDRATASE BOUND TO 4-DEOXYGLUCARATE
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-HOH:
WATER

ChemComp-GLR:
2,3-DIHYDROXY-5-OXO-HEXANEDIOATE

ChemComp-XYH:
XYLAROHYDROXAMATE

ChemComp-DXG:
4-DEOXYGLUCARATE

Source
  • escherichia coli (E. coli)
KeywordsLYASE / Glucarate Dehydratase Enolase Enzyme Superfamily TIM Barrel (beta/alpha)7beta barrel

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