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BioLiP

Structure of PDB 3qvi Chain D

Receptor sequence
>3qviD (length=327) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
EFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSES
CESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYK
FIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQ
AVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHF
GNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGN
TKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVL
GDPFMRKYFTVYDYDNHTVGFALAKNL
3D structure
PDB3qvi Structural insights into the activation and inhibition of histo-aspartic protease from Plasmodium falciparum.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H32 S35 N37 W39 S75 D215 T218
Catalytic site (residue number reindexed from 1) H33 S36 N38 W40 S76 D213 T216
Enzyme Commision number 3.4.23.39: plasmepsin II.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 K95 D E278A L281 E277 L283
BS02 K95 D H32 A34 S35 W39 L73 M189 H33 A35 S36 W40 L74 M191
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0044002 acquisition of nutrients from host
Cellular Component
GO:0005773 vacuole
GO:0005775 vacuolar lumen
GO:0016020 membrane
GO:0020020 food vacuole

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Molecular Function
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Cellular Component
External links
PDB RCSB:3qvi, PDBe:3qvi, PDBj:3qvi
PDBsum3qvi
PubMed21928835
UniProtQ9Y006|PLM3_PLAFX Plasmepsin III (Gene Name=PMIII)

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