Structure of PDB 2eph Chain D

Receptor sequence

>2ephD (length=351) Species: 5833 (Plasmodium falciparum)

CTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNI
KLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLL
HNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKW
RTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGP
HSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTT
QDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWA
LTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGA
G

3D structure

• PDB: 2eph Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite.
• Chain: D
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D39 K151 E194 E196 K236 S306
• Catalytic site (residue number reindexed from 1): D37 K149 E192 E194 K234 S304
• 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	D	E40 R48 K151 R153 R309 Q312 A313	E38 R46 K149 R151 R307 Q310 A311

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:0030388 fructose 1,6-bisphosphate metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0016020 membrane
• GO:0020002 host cell plasma membrane

External links

• PDB: RCSB:2eph, PDBe:2eph, PDBj:2eph
• PDBsum: 2eph
• PubMed: 17426153
• UniProt: P14223|ALF_PLAFA Fructose-bisphosphate aldolase (Gene Name=FBPA)