Structure of PDB 2xrf Chain B Binding Site BS01
Receptor Information
>2xrf Chain B (length=288) Species:
9606
(Homo sapiens) [
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RFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMK
AFALFMHKELGFEIKDICAGTDRYCMYKTGPVLAISHGMGIPSISIMLHE
LIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVI
LDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLD
GALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVT
LLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLGL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
2xrf Chain B Residue 400 [
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Receptor-Ligand Complex Structure
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PDB
2xrf
Crystal Structure of Human Uridine Phosphorylase 2
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
D93 C95 T98 Y101
Binding residue
(residue number reindexed from 1)
D66 C68 T71 Y74
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E127 R281
Catalytic site (residue number reindexed from 1)
E100 R254
Enzyme Commision number
2.4.2.3
: uridine phosphorylase.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2xrf
,
PDBe:2xrf
,
PDBj:2xrf
PDBsum
2xrf
PubMed
UniProt
O95045
|UPP2_HUMAN Uridine phosphorylase 2 (Gene Name=UPP2)
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