Structure of PDB 1seh Chain A Binding Site BS01

Receptor Information
>1seh Chain A (length=140) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTL
VPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMIS
VWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATR
Ligand information
Ligand IDUMP
InChIInChI=1S/C9H13N2O8P/c12-5-3-8(11-2-1-7(13)10-9(11)14)19-6(5)4-18-20(15,16)17/h1-2,5-6,8,12H,3-4H2,(H,10,13,14)(H2,15,16,17)/t5-,6+,8+/m0/s1
InChIKeyJSRLJPSBLDHEIO-SHYZEUOFSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=P(O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)CC2O
CACTVS 3.370O[CH]1C[CH](O[CH]1CO[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.6C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)COP(=O)(O)O)O
CACTVS 3.370O[C@H]1C[C@@H](O[C@@H]1CO[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.6C1C(C(OC1N2C=CC(=O)NC2=O)COP(=O)(O)O)O
FormulaC9 H13 N2 O8 P
Name2'-DEOXYURIDINE 5'-MONOPHOSPHATE;
DUMP
ChEMBLCHEMBL211312
DrugBankDB03800
ZINCZINC000004228260
PDB chain1seh Chain A Residue 777 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1seh Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase
Resolution1.47 Å
Binding residue
(original residue number in PDB)		M68 N84 G87 L88 I89 D90 Y93 M98
Binding residue
(residue number reindexed from 1)		M68 N84 G87 L88 I89 D90 Y93 M98
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) A29 R71 G73 I80 D90
Catalytic site (residue number reindexed from 1) A29 R71 G73 I80 D90
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:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0009117 nucleotide metabolic process
GO:0046081 dUTP catabolic process
GO:0070207 protein homotrimerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1seh, PDBe:1seh, PDBj:1seh
PDBsum1seh
PubMed15208312
UniProtP06968|DUT_ECOLI Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=dut)

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