Structure of PDB 1lzo Chain B

Receptor sequence
>1lzoB (length=246) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTR
KLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYF
HETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVD
LIDNFDNVILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQAN
QIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
3D structure
PDB1lzo 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
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B K12 S211 G232 N233 K10 S209 G230 N231 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

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Cellular Component
External links
PDB RCSB:1lzo, PDBe:1lzo, PDBj:1lzo
PDBsum1lzo
PubMed12403619
UniProtQ07412|TPIS_PLAFA Triosephosphate isomerase (Gene Name=TPI)

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