Structure of PDB 1w0m Chain E Binding Site BS01

Receptor Information
>1w0m Chain E (length=225) Species: 2271 (Thermoproteus tenax) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRLPILIINFKAYGEAAGKRAVELAKAAERAARELGVNIVVAPNHLELGL
VSQSVDIPVYAQGADVEAGGAHTAHVSLENIKEAGGSGVILNHSEAPLKL
NDLARLVAKAKSLGLDVVVCAPDPRTSLAAAALGPHAVAVEPPELIGTGR
AVSRYKPEAIVETVGLVSRHFPEVSVITGAGIESGDDVAAALRLGTRGVL
LASAAVKAKDPYAKIVELAKPLSEL
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1w0m Chain E Residue 1226 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1w0m Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature
Resolution2.5 Å
Binding residue
(original residue number in PDB)		I146 G147 A202 S203
Binding residue
(residue number reindexed from 1)		I146 G147 A202 S203
Annotation score1
Enzymatic activity
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:1w0m, PDBe:1w0m, PDBj:1w0m
PDBsum1w0m
PubMed15342242
UniProtQ8NKN9|TPIS_THETK Triosephosphate isomerase (Gene Name=tpiA)

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