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Structure paper

TitleThe structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Journal, issue, pagesBiochemistry, Vol. 34, Page 13612-13621, Year 1995
Publish dateFeb 3, 1994 (structure data deposition date)
AuthorsKomives, E.A. / Lougheed, J.C. / Liu, K. / Sugio, S. / Zhang, Z. / Petsko, G.A. / Ringe, D.
External linksBiochemistry / PubMed:7577950
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1tpb:
OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1tpc:
OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PGH:
PHOSPHOGLYCOLOHYDROXAMIC ACID

ChemComp-HOH:
WATER

Source
  • gallus gallus (chicken)
KeywordsISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)

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