Structure of PDB 3p0e Chain C

Receptor sequence
>3p0eC (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
FVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKA
FALFMHKELGFEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPSISI
MLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRF
EQVILDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQ
GRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAV
VCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLG
3D structure
PDB3p0e A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E127 R281
Catalytic site (residue number reindexed from 1) E104 R258
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 BAU C S148 G149 F219 Q223 R225 E254 I287 S125 G126 F196 Q200 R202 E231 I264
BS02 PO4 C G66 R144 T147 G43 R121 T124
BS03 BAU C Y41 H42 Y18 H19
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004850 uridine phosphorylase activity
GO:0005515 protein binding
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0042802 identical protein binding
GO:0047847 deoxyuridine phosphorylase activity
Biological Process
GO:0006218 uridine catabolic process
GO:0006249 dCMP catabolic process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0009166 nucleotide catabolic process
GO:0044206 UMP salvage
GO:0046108 uridine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0045098 type III intermediate filament

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Cellular Component
External links
PDB RCSB:3p0e, PDBe:3p0e, PDBj:3p0e
PDBsum3p0e
PubMed21855639
UniProtO95045|UPP2_HUMAN Uridine phosphorylase 2 (Gene Name=UPP2)

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