Structure of PDB 4tr9 Chain B Binding Site BS01

Receptor Information

>4tr9 Chain B (length=347) Species: 36329 (Plasmodium falciparum 3D7)

EYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKL
ENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHN
ENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRT
VLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHS
IEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQD
VGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALT
FSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGG

Ligand information

>4tr9 Chain G (length=11) Species: 36329 (Plasmodium falciparum 3D7)

AAASLYEKKAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4tr9 Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex.
• Resolution: 2.111 Å
• Binding residue (original residue number in PDB): F257 R261 R264 L296 G297 P298
• Binding residue (residue number reindexed from 1): F253 R257 R260 L292 G293 P294

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

External links

• PDB: RCSB:4tr9, PDBe:4tr9, PDBj:4tr9
• PDBsum: 4tr9
• PubMed: 26289816
• UniProt: Q7KQL9|ALF_PLAF7 Fructose-bisphosphate aldolase (Gene Name=FBPA)