Structure of PDB 3p48 Chain B Binding Site BS02

Receptor Information
>3p48 Chain B (length=126) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVLKIQLRSASATVPTKGSATAAGYDIYASQDITIPAMGQGMVSTDISFT
VPVGTYGRIAPRSGLAVKNGIQTGAGVVDRDYTGEVKVVLFNHSQRDFAI
KKGDRVAQLILEKIVDDAQIVVVDSL
Ligand information
Ligand IDDUP
InChIInChI=1S/C9H16N3O13P3/c13-5-3-8(12-2-1-7(14)10-9(12)15)24-6(5)4-23-26(16,17)11-27(18,19)25-28(20,21)22/h1-2,5-6,8,13H,3-4H2,(H,10,14,15)(H2,20,21,22)(H3,11,16,17,18,19)/t5-,6+,8+/m0/s1
InChIKeyXZLLMTSKYYYJLH-SHYZEUOFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C(C(OC1N2C=CC(=O)NC2=O)COP(=O)(NP(=O)(O)OP(=O)(O)O)O)O
CACTVS 3.341O[C@H]1C[C@@H](O[C@@H]1CO[P@](O)(=O)N[P@](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.5.0C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)CO[P@](=O)(N[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.341O[CH]1C[CH](O[CH]1CO[P](O)(=O)N[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)NP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)CC2O
FormulaC9 H16 N3 O13 P3
Name2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE
ChEMBLCHEMBL1232397
DrugBankDB01965
ZINC
PDB chain3p48 Chain B Residue 149 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3p48 Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.
Resolution1.67 Å
Binding residue
(original residue number in PDB)		A81 G82 V83 D85 Y88 K93
Binding residue
(residue number reindexed from 1)		A75 G76 V77 D79 Y82 K87
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) A29 R68 G70 I77 D85
Catalytic site (residue number reindexed from 1) A23 R62 G64 I71 D79
Enzyme Commision number 3.6.1.23: dUTP diphosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004170 dUTP diphosphatase activity
GO:0016787 hydrolase activity
GO:0035870 dITP diphosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0009117 nucleotide metabolic process
GO:0009213 pyrimidine deoxyribonucleoside triphosphate catabolic process
GO:0035863 dITP catabolic process
GO:0046081 dUTP catabolic process
Cellular Component
GO:0005634 nucleus
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:3p48, PDBe:3p48, PDBj:3p48
PDBsum3p48
PubMed21548881
UniProtP33317|DUT_YEAST Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=DUT1)

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