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Structure of PDB 1btm Chain B Binding Site BS01

Receptor Information >1btm Chain B (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 ID PGA InChI InChI=1S/C2H5O6P/c3-2(4)1-8-9(5,6)7/h1H2,(H,3,4)(H2,5,6,7) InChIKey ASCFNMCAHFUBCO-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 OC(=O)CO[P](O)(O)=O OpenEye OEToolkits 1.5.0 C(C(=O)O)OP(=O)(O)O ACDLabs 10.04 O=P(O)(O)OCC(=O)O Formula C2 H5 O6 P Name 2-PHOSPHOGLYCOLIC ACID ChEMBL CHEMBL47181 DrugBank DB02726 ZINC ZINC000003869735 PDB chain 1btm Chain B Residue 570 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1btm 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. Resolution 2.8 Å Binding residue (original residue number in PDB) K10 H94 E166 I171 G172 G211 S212 G233 Binding residue (residue number reindexed from 1) K10 H94 E166 I171 G172 G211 S212 G233 Annotation score 2

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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