Structure of PDB 1odl Chain A Binding Site BS02
Receptor Information
>1odl Chain A (length=234) Species:
300852
(Thermus thermophilus HB8) [
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SPIHVRAHPGDVAERVLLPGDPGRAEWIAKTFLQNPRRYNDHRGLWGYTG
LYKGVPVSVQTTGMGTPSAAIVVEELVRLGARVLVRVGTAGAASSDLAPG
ELIVAQGAVPLDGTTRQYLEGRPYAPVPDPEVFRALWRRAEALGYPHRVG
LVASEDAFYATTPEEARAWARYGVLAFEMEASALFLLGRMRGVRTGAILA
VSNRIGDPELAPPEVLQEGVRRMVEVALEAVLEV
Ligand information
Ligand ID
SO4
InChI
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKey
QAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[O-]S(=O)(=O)[O-]
CACTVS 3.341
[O-][S]([O-])(=O)=O
ACDLabs 10.04
[O-]S([O-])(=O)=O
Formula
O4 S
Name
SULFATE ION
ChEMBL
DrugBank
DB14546
ZINC
PDB chain
1odl Chain A Residue 1237 [
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Receptor-Ligand Complex Structure
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PDB
1odl
Crystal Structure of Purine Nucleoside Phosphorylase from Thermus Thermophilus
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
R135 R139
Binding residue
(residue number reindexed from 1)
R134 R138
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H5 G21 R25 R44 E76 R87 T90 S203 N204 I206 L217
Catalytic site (residue number reindexed from 1)
H4 G20 R24 R43 E75 R86 T89 S202 N203 I205 L216
Enzyme Commision number
2.4.2.3
: uridine phosphorylase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0016757
glycosyltransferase activity
GO:0016763
pentosyltransferase activity
Biological Process
GO:0009116
nucleoside metabolic process
GO:0009164
nucleoside catabolic process
Cellular Component
GO:0005829
cytosol
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Molecular Function
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Cellular Component
External links
PDB
RCSB:1odl
,
PDBe:1odl
,
PDBj:1odl
PDBsum
1odl
PubMed
15046984
UniProt
Q5SID9
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