Structure of PDB 1odi Chain A

Receptor sequence
>1odiA (length=234) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
SPIHVRAHPGDVAERVLLPGDPGRAEWIAKTFLQNPRRYNDHRGLWGYTG
LYKGVPVSVQTTGMGTPSAAIVVEELVRLGARVLVRVGTAGAASSDLAPG
ELIVAQGAVPLDGTTRQYLEGRPYAPVPDPEVFRALWRRAEALGYPHRVG
LVASEDAFYATTPEEARAWARYGVLAFEMEASALFLLGRMRGVRTGAILA
VSNRIGDPELAPPEVLQEGVRRMVEVALEAVLEV
3D structure
PDB1odi Crystal Structure of Purine Nucleoside Phosphorylase from Thermus Thermophilus
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SO4 A G21 R25 R87 G89 T90 G20 R24 R86 G88 T89
BS02 ADN A M65 T90 A91 G92 E156 F159 F178 E179 M180 E181 N204 M64 T89 A90 G91 E155 F158 F177 E178 M179 E180 N203 MOAD: Kd=62uM
PDBbind-CN: -logKd/Ki=4.21,Kd=62uM
BS03 ADN A H5 R44 H4 R43 MOAD: Kd=62uM
PDBbind-CN: -logKd/Ki=4.21,Kd=62uM
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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Cellular Component
External links
PDB RCSB:1odi, PDBe:1odi, PDBj:1odi
PDBsum1odi
PubMed15046984
UniProtQ5SID9

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