Structure of PDB 2hqu Chain A Binding Site BS02
Receptor Information
>2hqu Chain A (length=138) Species:
9606
(Homo sapiens) [
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MQLRFARLSEHATAPTRRAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPS
GCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKG
DRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
Ligand information
Ligand ID
DUP
InChI
InChI=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
InChIKey
XZLLMTSKYYYJLH-SHYZEUOFSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C1C(C(OC1N2C=CC(=O)NC2=O)COP(=O)(NP(=O)(O)OP(=O)(O)O)O)O
CACTVS 3.341
O[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 1.5.0
C1[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 3.341
O[CH]1C[CH](O[CH]1CO[P](O)(=O)N[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)NP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)CC2O
Formula
C9 H16 N3 O13 P3
Name
2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE
ChEMBL
CHEMBL1232397
DrugBank
DB01965
ZINC
PDB chain
2hqu Chain B Residue 777 [
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Receptor-Ligand Complex Structure
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PDB
2hqu
Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
A98 G99 V100 I101 D102 Y105 G110
Binding residue
(residue number reindexed from 1)
A72 G73 V74 I75 D76 Y79 G84
Annotation score
3
Binding affinity
MOAD
: 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)
A20 R59 G61 I68 D76
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
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Biological Process
External links
PDB
RCSB:2hqu
,
PDBe:2hqu
,
PDBj:2hqu
PDBsum
2hqu
PubMed
17880943
UniProt
P33316
|DUT_HUMAN Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (Gene Name=DUT)
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