Literature summary for 3.4.23.B14 extracted from

Silva, N.; Lameira, J.; Alves, C.
A quantum mechanical/molecular mechanical study of the aspartic protease plasmepsin IV complexed with allophenylnorstatine-based inhibitor (2011), Chem. Phys. Lett., 509, 169-174.

No PubMed abstract available

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Crystallization (Commentary)

Crystallization (Comment)	Organism
pKa calculations for PM IV complexed with the inhibitor KNI-764. Residue Asp214 is protonated, while residue Asp34 is deprotonated. In the colmplex, the hydroxyl group interacts with the OD2 oxygen atom of Asp34 through a hydrogen bond. The hydroxyl group also presents a hydrogen bond interaction with acid aspartic protonated Asp214. The amino groups of Gly78 and Ser79 residues interact with KNI-764 forming hydrogen bonds at 2.02 and 2.20 A. The hydroxyl group of Thr217 forms hydrogen bonds with the inhibitor at 2.06 A	Plasmodium malariae

Crystallization (Comment)

Organism

pKa calculations for PM IV complexed with the inhibitor KNI-764. Residue Asp214 is protonated, while residue Asp34 is deprotonated. In the colmplex, the hydroxyl group interacts with the OD2 oxygen atom of Asp34 through a hydrogen bond. The hydroxyl group also presents a hydrogen bond interaction with acid aspartic protonated Asp214. The amino groups of Gly78 and Ser79 residues interact with KNI-764 forming hydrogen bonds at 2.02 and 2.20 A. The hydroxyl group of Thr217 forms hydrogen bonds with the inhibitor at 2.06 A

Plasmodium malariae

Organism

Organism	UniProt	Comment	Textmining
Plasmodium malariae	O60990	-	-

Synonyms

Synonyms	Comment	Organism
PM IV	-	Plasmodium malariae

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Release 2023.1 (January 2023)