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Structure paper

TitleEvolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli.
Journal, issue, pagesBiochemistry, Vol. 40, Page 10054-10062, Year 2001
Publish dateJun 11, 2001 (structure data deposition date)
AuthorsGulick, A.M. / Hubbard, B.K. / Gerlt, J.A. / Rayment, I.
External linksBiochemistry / PubMed:11513584
MethodsX-ray diffraction
Resolution2 - 2.75 Å
Structure data

PDB-1jct:
Glucarate Dehydratase, N341L mutant Orthorhombic Form
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-1jdf:
Glucarate Dehydratase from E.coli N341D mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GKR:
D-GLUCARATE

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-HOH:
WATER

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

Source
  • escherichia coli (E. coli)
KeywordsLYASE / alpha/beta barrel / Enolase superfamily / TIM Barrel

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