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BioLiP

Structure of PDB 4tr9 Chain A Binding Site BS02

Receptor Information
>4tr9 Chain A (length=347) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKL
ENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHN
ENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRT
VLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHS
IEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQD
VGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALT
FSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGG
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4tr9 Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex.
Resolution2.111 Å
Binding residue
(original residue number in PDB)		E40 R48 E196 S278 G279 G308 R309
Binding residue
(residue number reindexed from 1)		E36 R44 E192 S274 G275 G304 R305
Enzymatic activity
Catalytic site (original residue number in PDB) D39 K151 E194 E196 K236 S306
Catalytic site (residue number reindexed from 1) D35 K147 E190 E192 K232 S302
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
Gene Ontology
Molecular Function
GO:0003779 actin binding
GO:0004332 fructose-bisphosphate aldolase activity
GO:0016829 lyase activity
Biological Process
GO:0006096 glycolytic process
GO:0008154 actin polymerization or depolymerization
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane
GO:0020002 host cell plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4tr9, PDBe:4tr9, PDBj:4tr9
PDBsum4tr9
PubMed26289816
UniProtQ7KQL9|ALF_PLAF7 Fructose-bisphosphate aldolase (Gene Name=FBPA)

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