Structure of PDB 2j27 Chain B Binding Site BS01

Receptor Information
>2j27 Chain B (length=249) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAY
YGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIA
KKLKKADWAKVVIAYEAVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD
VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
Ligand information
Ligand IDPGA
InChIInChI=1S/C2H5O6P/c3-2(4)1-8-9(5,6)7/h1H2,(H,3,4)(H2,5,6,7)
InChIKeyASCFNMCAHFUBCO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(C(=O)O)OP(=O)(O)O
ACDLabs 10.04O=P(O)(O)OCC(=O)O
FormulaC2 H5 O6 P
Name2-PHOSPHOGLYCOLIC ACID
ChEMBLCHEMBL47181
DrugBankDB02726
ZINCZINC000003869735
PDB chain2j27 Chain B Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2j27 Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Resolution1.15 Å
Binding residue
(original residue number in PDB)		K13 H95 E167 I172 G212 S213 G234 G235
Binding residue
(residue number reindexed from 1)		K12 H94 E166 I171 G211 S212 G233 G234
Annotation score2
Binding affinityMOAD: Ki=0.3mM
PDBbind-CN: -logKd/Ki=3.52,Ki=0.3mM
Enzymatic activity
Catalytic site (original residue number in PDB) N11 K13 H95 E97 E167 G173 S213
Catalytic site (residue number reindexed from 1) N10 K12 H94 E96 E166 G172 S212
Enzyme Commision number 5.3.1.1: triose-phosphate isomerase.
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019563 glycerol catabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2j27, PDBe:2j27, PDBj:2j27
PDBsum2j27
PubMed17176070
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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