Structure of PDB 6hde Chain A

Receptor sequence
>6hdeA (length=148) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTL
VPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYHGQLMIS
VWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFRGEGGFGHSGRQ
3D structure
PDB6hde The Role of a Key Amino Acid Position in Species-Specific Proteinaceous dUTPase Inhibition.
ChainA
Resolution1.82 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.23: dUTP diphosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 DUP A R71 S72 G73 Q119 R71 S72 G73 Q119 MOAD: Kd=60.8nM
BS02 DUP A R141 G145 F146 G147 H148 S149 R137 G141 F142 G143 H144 S145 MOAD: Kd=60.8nM
BS03 DUP A N84 I89 D90 Y93 M98 N84 I89 D90 Y93 M98 MOAD: Kd=60.8nM
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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Cellular Component
External links
PDB RCSB:6hde, PDBe:6hde, PDBj:6hde
PDBsum6hde
PubMed31174420
UniProtP06968|DUT_ECOLI Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=dut)

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