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1QDS

SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM)

Summary for 1QDS
Entry DOI10.2210/pdb1qds/pdb
Related1AMK
DescriptorTRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total)
Functional Keywordstim, leishmania, stability, mutagenesis, pka, isomerase
Biological sourceLeishmania mexicana
Cellular locationCytoplasm: P48499
Total number of polymer chains1
Total formula weight27364.27
Authors
Lambeir, A.M.,Backmann, J.,Ruiz-Sanz, J.,Filimonov, V.,Nielsen, J.E.,Vriend, G.,Kursula, I.,Norledge, B.V.,Wierenga, R.K. (deposition date: 1999-07-10, release date: 2000-12-13, Last modification date: 2024-02-14)
Primary citationLambeir, A.M.,Backmann, J.,Ruiz-Sanz, J.,Filimonov, V.,Nielsen, J.E.,Kursula, I.,Norledge, B.V.,Wierenga, R.K.
The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
Eur.J.Biochem., 267:2516-2524, 2000
Cited by
PubMed: 10785370
DOI: 10.1046/j.1432-1327.2000.01254.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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