Structure of PDB 1lyx Chain A

Receptor sequence

>1lyxA (length=246) Species: 5833 (Plasmodium falciparum)

RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTR
KLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYF
HETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVD
LIDNFDNVILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQAN
QIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM

3D structure

• PDB: 1lyx Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N10 K12 H95 E97 E165 G171 S211
• Catalytic site (residue number reindexed from 1): N8 K10 H93 E95 E163 G169 S209
• Enzyme Commision number: 5.3.1.1: triose-phosphate isomerase.

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	PGA	A	K12 H95 E165 I170 G171 G210 S211 G232 N233	K10 H93 E163 I168 G169 G208 S209 G230 N231	MOAD: Ki=0.029mM PDBbind-CN: -logKd/Ki=4.54,Ki=0.029mM

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity
• GO:0016853 isomerase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0019563 glycerol catabolic process
• GO:0046166 glyceraldehyde-3-phosphate biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1lyx, PDBe:1lyx, PDBj:1lyx
• PDBsum: 1lyx
• PubMed: 12403619
• UniProt: Q07412|TPIS_PLAFA Triosephosphate isomerase (Gene Name=TPI)