Literature summary for 2.3.1.282 extracted from

Buglino, J.; Onwueme, K.C.; Ferreras, J.A.; Quadri, L.E.; Lima, C.D.
Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis (2004), J. Biol. Chem., 279, 30634-30642 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.75 A resoultion. The PapA5 active site includes conserved histidine and aspartic acid residues that are critical to PapA5 acyltransferase activity. Two hydrophobic channels link the PapA5 surface to the active. An additional alpha helix blocks the putative entrance into the PapA5 active site	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WIN5	-	-
Mycobacterium tuberculosis H37Rv	P9WIN5	-	-

Synonyms

Synonyms	Comment	Organism
papA5	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)