Structure of PDB 1smc Chain B Binding Site BS01

Receptor Information
>1smc Chain B (length=138) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMSTTLAIVRLDPGLPLPSRAHDGDAGVDLYSAEDVELAPGRRALVRTGV
AVAVPFGMVGLVHPRSGLATRVGLSIVNSPGTIDAGYRGEIKVALINLDP
AAPIVVHRGDRIAQLLVQRVELVELVEVSSFDEAGLAR
Ligand information
Ligand IDDUT
InChIInChI=1S/C9H15N2O14P3/c12-5-3-8(11-2-1-7(13)10-9(11)14)23-6(5)4-22-27(18,19)25-28(20,21)24-26(15,16)17/h1-2,5-6,8,12H,3-4H2,(H,18,19)(H,20,21)(H,10,13,14)(H2,15,16,17)/t5-,6+,8+/m0/s1
InChIKeyAHCYMLUZIRLXAA-SHYZEUOFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O
OpenEye OEToolkits 1.5.0C1C(C(OC1N2C=CC(=O)NC2=O)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O
CACTVS 3.341O[CH]1C[CH](O[CH]1CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.341O[C@H]1C[C@@H](O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)CC2O
FormulaC9 H15 N2 O14 P3
NameDEOXYURIDINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL374361
DrugBankDB02333
ZINCZINC000008215971
PDB chain1smc Chain A Residue 2170 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1smc Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		N77 T81 I82 D83 Y86 K91
Binding residue
(residue number reindexed from 1)		N78 T82 I83 D84 Y87 K92
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A25 R64 G66 L73 D83
Catalytic site (residue number reindexed from 1) A26 R65 G67 L74 D84
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:0046872 metal ion binding
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0009117 nucleotide metabolic process
GO:0046080 dUTP metabolic process
GO:0046081 dUTP catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1smc, PDBe:1smc, PDBj:1smc
PDBsum1smc
PubMed15276840
UniProtP9WNS5|DUT_MYCTU Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=dut)

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