Structure of PDB 1lf2 Chain A

Receptor sequence
>1lf2A (length=329) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
SSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTA
GCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPY
KFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIE
NALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAH
VGNISLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCN
NSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFI
LGDPFMRKYFTVFDYDNHSVGIALAKKNL
3D structure
PDB1lf2 Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 A in complex with the inhibitors rs367 and rs370.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D34 S37 N39 W41 Y77 D214 T217
Catalytic site (residue number reindexed from 1) D34 S37 N39 W41 Y77 D214 T217
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 R37 A D34 G36 N76 Y77 V78 S79 F111 I123 Y192 D214 G216 T217 S218 F294 D34 G36 N76 Y77 V78 S79 F111 I123 Y192 D214 G216 T217 S218 F294 PDBbind-CN: -logKd/Ki=7.52,Ki=30nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1lf2, PDBe:1lf2, PDBj:1lf2
PDBsum1lf2
PubMed12454457
UniProtP46925|PLM2_PLAFX Plasmepsin II (Gene Name=PMII)

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