Structure of PDB 1w0m Chain H Binding Site BS01

Receptor Information
>1w0m Chain H (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 H 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 L201 A202 S203
Binding residue
(residue number reindexed from 1)
I146 G147 L201 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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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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