Structure of PDB 1o5x Chain A Binding Site BS01
Receptor Information
>1o5x Chain A (length=246) Species:
5833
(Plasmodium falciparum) [
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RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTR
KLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYF
HETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVD
LIDNFDNVILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQAN
QIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
Ligand information
Ligand ID
PO3
InChI
InChI=1S/O3P/c1-4(2)3/q-3
InChIKey
AQSJGOWTSHOLKH-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[O-][P-]([O-])=O
ACDLabs 10.04
[O-][PH2-]([O-])=O
OpenEye OEToolkits 1.5.0
[O-][P-](=O)[O-]
Formula
O3 P
Name
PHOSPHITE ION
ChEMBL
DrugBank
ZINC
PDB chain
1o5x Chain A Residue 6000 [
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Receptor-Ligand Complex Structure
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PDB
1o5x
Structure of Plasmodium falciparum Triose-phosphate Isomerase-2-Phosphoglycerate Complex at 1.1-A Resolution
Resolution
1.1 Å
Binding residue
(original residue number in PDB)
G232 N233
Binding residue
(residue number reindexed from 1)
G230 N231
Annotation score
1
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.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1o5x
,
PDBe:1o5x
,
PDBj:1o5x
PDBsum
1o5x
PubMed
14563846
UniProt
Q07412
|TPIS_PLAFA Triosephosphate isomerase (Gene Name=TPI)
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