Structure of PDB 4tr9 Chain B

Receptor sequence

>4tr9B (length=347) Species: 36329 (Plasmodium falciparum 3D7)

EYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKL
ENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHN
ENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRT
VLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHS
IEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQD
VGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALT
FSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGG

3D structure

• PDB: 4tr9 Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex.
• Chain: B
• Resolution: 2.111 Å

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.

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	B	F257 R261 R264 L296 G297 P298	F253 R257 R260 L292 G293 P294
BS02	peptide	B	A37 E40 R48 E196 S278 G279 G308 R309 Q312	A33 E36 R44 E192 S274 G275 G304 R305 Q308
BS03	38D	B	D39 S41 T44 K47 K112 K151	D35 S37 T40 K43 K108 K147

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)