Structure of PDB 1hti Chain B Binding Site BS01

Receptor Information
>1hti Chain B (length=248) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDF
ARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRH
VFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVI
ADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAV
AQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
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 chain1hti Chain B Residue 549 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1hti Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		N11 K13 H95 E165 I170 G210 L230 G232
Binding residue
(residue number reindexed from 1)		N11 K13 H95 E165 I170 G210 L230 G232
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=5.13,Ki=7.4uM
Enzymatic activity
Catalytic site (original residue number in PDB) N11 K13 H95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N11 K13 H95 E97 E165 G171 S211
Enzyme Commision number 4.2.3.3: methylglyoxal synthase.
5.3.1.1: triose-phosphate isomerase.
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0005515 protein binding
GO:0008929 methylglyoxal synthase activity
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0031625 ubiquitin protein ligase binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006006 glucose metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019242 methylglyoxal biosynthetic process
GO:0019563 glycerol catabolic process
GO:0019682 glyceraldehyde-3-phosphate metabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
GO:0061621 canonical glycolysis
Cellular Component
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hti, PDBe:1hti, PDBj:1hti
PDBsum1hti
PubMed8061610
UniProtP60174|TPIS_HUMAN Triosephosphate isomerase (Gene Name=TPI1)

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