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1AMK

LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE

Summary for 1AMK
Entry DOI10.2210/pdb1amk/pdb
DescriptorTRIOSE PHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total)
Functional Keywordstim, 2-pg, pga, gluconeogenesis, fatty acid biosynthesis
Biological sourceLeishmania mexicana
Cellular locationCytoplasm: P48499
Total number of polymer chains1
Total formula weight27365.25
Authors
Williams, J.C.,Wierenga, R. (deposition date: 1997-06-17, release date: 1997-12-17, Last modification date: 2023-08-02)
Primary citationWilliams, J.C.,Zeelen, J.P.,Neubauer, G.,Vriend, G.,Backmann, J.,Michels, P.A.,Lambeir, A.M.,Wierenga, R.K.
Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
Protein Eng., 12:243-250, 1999
Cited by
PubMed: 10235625
DOI: 10.1093/protein/12.3.243
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.83 Å)
Structure validation

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