Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data Bank

Acta Crystallographica Section D: Biological Crystallography

Volumn 65, Issue 3, 2009, Pages 294-296

  Robbins, Arthur H ^a   Dunn, Ben M ^a   Agbandje Mckenna, Mavis ^a   McKenna, Robert ^a  

^a UNIVERSITY OF FLORIDA   (United States)

Author keywords

Catalytic mechanism; Nucleophiles; Plasmepsin II; Plasmodium falciparum

Indexed keywords

ASPARTIC ACID; ASPARTIC PROTEINASE; PLASMEPSIN II; PROTOZOAL PROTEIN; WATER;

ANIMAL; ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ELECTRON; ENZYME ACTIVE SITE; ENZYMOLOGY; HYDROGEN BOND; PLASMODIUM FALCIPARUM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; ASPARTIC ACID; ASPARTIC ENDOPEPTIDASES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; HYDROGEN BONDING; MODELS, MOLECULAR; PLASMODIUM FALCIPARUM; PROTEIN CONFORMATION; PROTOZOAN PROTEINS; WATER;

PLASMODIUM FALCIPARUM;

EID: 61349188242     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444908041632     Document Type: Article

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