Structure of PDB 1m43 Chain A

Receptor sequence
>1m43A (length=331) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
LGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCT
TAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSL
PYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNK
IENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLD
AHVGNISLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTL
CNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPT
FILGDPFMRKYFTVFDYDNHSVGIALAKKNL
3D structure
PDB1m43 Novel uncomplexed and complex structures of PM II, an aspartic protease from P. falciparum
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D34 S37 N39 W41 Y77 D214 T217
Catalytic site (residue number reindexed from 1) D36 S39 N41 W43 Y79 D216 T219
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 peptide A M15 I32 D34 G36 N76 Y77 V78 S79 Y192 D214 G216 T217 S218 M17 I34 D36 G38 N78 Y79 V80 S81 Y194 D216 G218 T219 S220
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1m43, PDBe:1m43, PDBj:1m43
PDBsum1m43
PubMed
UniProtP46925|PLM2_PLAFX Plasmepsin II (Gene Name=PMII)

[Back to BioLiP]