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Structure paper

TitleConformational Flexibility of PEP Mutase
Journal, issue, pagesBiochemistry, Vol. 43, Page 4447-4453, Year 2004
Publish dateJan 11, 2004 (structure data deposition date)
AuthorsLiu, S. / Lu, Z. / Han, Y. / Jia, Y. / Howard, A. / Dunaway-Mariano, D. / Herzberg, O.
External linksBiochemistry / PubMed:15078090
MethodsX-ray diffraction
Resolution1.69 - 2.1 Å
Structure data

PDB-1s2t:
Crystal Structure Of Apo Phosphoenolpyruvate Mutase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1s2u:
Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1s2v:
Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1s2w:
Crystal structure of phosphoenolpyruvate mutase in high ionic strength
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • mytilus edulis (blue mussel)
KeywordsISOMERASE / phosphoenolpyruvate mutase / PEP mutase / phosphonopyruvate / phosphonate biosynthesis pathway

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