Structure of PDB 3kvr Chain A Binding Site BS03
Receptor Information
>3kvr Chain A (length=293) Species:
9913
(Bos taurus) [
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LVQLCNPHIAAMKEDILYHFSLSTSTHDFPAMFGDVKFVCVGGSPSRMKA
FIKYVAMELGFAHPGADYPNICEGTDRYAMFKVGPVLSVSHGMGVPSIAI
MLHELIKLLYHAHCSGVTLIRIGTSGGIGLEPGSVVITRQAVDPCFKPEF
EQIVLGKREVRNTDLDEQLVQELARCSAELGEFPTVVGNTMCTLDFYEGQ
GRLDGALCSYTEKDKQDYLRAAYAAGIRNIEMEASVFAAMCNACGLRAAV
VCVTLLNRLEGDQISSPHDVLAEYQQRPQRLVGQFIKKRLMQA
Ligand information
Ligand ID
R2G
InChI
InChI=1S/C5H8O3/c6-3-5-4(7)1-2-8-5/h1-2,4-7H,3H2/t4-,5+/m1/s1
InChIKey
SGOSIWMWLVSBIC-UHNVWZDZSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 2.0.7
C1=COC(C1O)CO
CACTVS 3.385
OC[C@@H]1OC=C[C@H]1O
OpenEye OEToolkits 2.0.7
C1=CO[C@H]([C@@H]1O)CO
CACTVS 3.385
OC[CH]1OC=C[CH]1O
Formula
C5 H8 O3
Name
2,5-anhydro-4-deoxy-D-erythro-pent-4-enitol
ChEMBL
DrugBank
ZINC
PDB chain
3kvr Chain A Residue 311 [
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Receptor-Ligand Complex Structure
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PDB
3kvr
Glycal formation in crystals of uridine phosphorylase.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
M109 T140 E249
Binding residue
(residue number reindexed from 1)
M93 T124 E233
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E120 R274
Catalytic site (residue number reindexed from 1)
E104 R258
Enzyme Commision number
2.4.2.3
: uridine phosphorylase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004850
uridine phosphorylase activity
GO:0016757
glycosyltransferase activity
GO:0016763
pentosyltransferase activity
GO:0047847
deoxyuridine phosphorylase activity
Biological Process
GO:0009116
nucleoside metabolic process
GO:0009164
nucleoside catabolic process
GO:0009166
nucleotide catabolic process
GO:0044206
UMP salvage
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3kvr
,
PDBe:3kvr
,
PDBj:3kvr
PDBsum
3kvr
PubMed
20364833
UniProt
A5PJH9
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