Structure of PDB 1sw3 Chain A Binding Site BS01

Receptor Information
>1sw3 Chain A (length=247) Species: 9031 (Gallus gallus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFA
RQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHV
FGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIA
DNVKDWSKVVLAYEPVWAIGTGKVATPQQAQEVHEKLRGWLKSHVSDAVA
QSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
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 chain1sw3 Chain A Residue 350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1sw3 Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
Resolution2.03 Å
Binding residue
(original residue number in PDB)		K13 H95 E165 I170 G210 S211 L230 G232 G233
Binding residue
(residue number reindexed from 1)		K12 H94 E164 I169 G209 S210 L229 G231 G232
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) N11 K13 H95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N10 K12 H94 E96 E164 G170 S210
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: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: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:1sw3, PDBe:1sw3, PDBj:1sw3
PDBsum1sw3
PubMed15166315
UniProtP00940|TPIS_CHICK Triosephosphate isomerase (Gene Name=TPI1)

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