Structure of PDB 1w0m Chain C Binding Site BS01
Receptor Information
>1w0m Chain C (length=225) Species:
2271
(Thermoproteus tenax) [
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MRLPILIINFKAYGEAAGKRAVELAKAAERAARELGVNIVVAPNHLELGL
VSQSVDIPVYAQGADVEAGGAHTAHVSLENIKEAGGSGVILNHSEAPLKL
NDLARLVAKAKSLGLDVVVCAPDPRTSLAAAALGPHAVAVEPPELIGTGR
AVSRYKPEAIVETVGLVSRHFPEVSVITGAGIESGDDVAAALRLGTRGVL
LASAAVKAKDPYAKIVELAKPLSEL
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
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-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
1w0m Chain C Residue 1226 [
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Receptor-Ligand Complex Structure
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PDB
1w0m
Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
I146 G147 G181 A202 S203
Binding residue
(residue number reindexed from 1)
I146 G147 G181 A202 S203
Annotation score
1
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
PDBsum
1w0m
PubMed
15342242
UniProt
Q8NKN9
|TPIS_THETK Triosephosphate isomerase (Gene Name=tpiA)
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