Structure of PDB 2hqu Chain B Binding Site BS01

Receptor Information
>2hqu Chain B (length=141) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIA
LPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEV
KKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
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 chain2hqu Chain A Residue 777 [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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PDB2hqu Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		A98 G99 V100 I101 D102 Y105 G110
Binding residue
(residue number reindexed from 1)		A75 G76 V77 I78 D79 Y82 G87
Annotation score3
Binding affinityMOAD: Kd=7.2uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.2uM
Enzymatic activity
Catalytic site (original residue number in PDB) A46 R85 G87 I94 D102
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
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0046081 dUTP catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hqu, PDBe:2hqu, PDBj:2hqu
PDBsum2hqu
PubMed17880943
UniProtP33316|DUT_HUMAN Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (Gene Name=DUT)

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