Structure of PDB 1btm Chain A Binding Site BS01

Receptor Information
>1btm Chain A (length=251) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLV
QAADGTDLKIGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQM
FAETDETVNKKVLAAFTRGLIPIICCGESLEEREAGQTNAVVASQVEKAL
AGLTPEQVKQAVIAYEPIWAIGTGKSSTPEDANSVCGHIRSVVSRLFGPE
AAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEPASFLQLVEAGR
H
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 chain1btm Chain A Residue 560 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1btm Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		K10 H94 E166 I171 G172 S212 G233
Binding residue
(residue number reindexed from 1)		K10 H94 E166 I171 G172 S212 G233
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) N8 K10 H94 E96 E166 G172 S212
Catalytic site (residue number reindexed from 1) N8 K10 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1btm, PDBe:1btm, PDBj:1btm
PDBsum1btm
PubMed8580851
UniProtP00943|TPIS_GEOSE Triosephosphate isomerase (Gene Name=tpiA)

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