Literature summary for 5.3.1.6 extracted from

Capriles, P.V.; Baptista, L.P.; Guedes, I.A.; Guimaraes, A.C.; Custodio, F.L.; Alves-Ferreira, M.; Dardenne, L.E.
Structural modeling and docking studies of ribose 5-phosphate isomerase from Leishmania major and Homo sapiens a comparative analysis for Leishmaniasis treatment (2015), J. Mol. Graph. Model., 55, 134-147 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
comparison of structures and active sites of RpiB and RpiA from Homo sapiens (HsRpiA). Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes. In LmRpiB, residues Y46,H11, H102 and H138 are part of the active site	Leishmania major
comparison of structures and active sites of RpiB from Leishmania major and RpiA and docking of substrate. Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P49247	-	-
Leishmania major	Q4Q869	-	-

Synonyms

Synonyms	Comment	Organism
LMJF_28_1970	-	Leishmania major
RpiA	-	Homo sapiens
RpiB	-	Leishmania major

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Release 2023.1 (January 2023)