Structure of PDB 3p48 Chain A

Receptor sequence
>3p48A (length=127) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KVLKIQLRSASATVPTKGSATAAGYDIYASQDITIPAMGQGMVSTDISFT
VPVGTYGRIAPRSGLAVKNGIQTGAGVVDRDYTGEVKVVLFNHSQRDFAI
KKGDRVAQLILEKIVDDAQIVVVDSLE
3D structure
PDB3p48 Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.
ChainA
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A29 R68 G70 I77 D85
Catalytic site (residue number reindexed from 1) A23 R62 G64 I71 D79
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 R68 S69 G70 R62 S63 G64
BS02 DUP A G82 V83 D85 Y88 K93 G76 V77 D79 Y82 K87
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004170 dUTP diphosphatase activity
GO:0016787 hydrolase activity
GO:0035870 dITP diphosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0009117 nucleotide metabolic process
GO:0009213 pyrimidine deoxyribonucleoside triphosphate catabolic process
GO:0035863 dITP catabolic process
GO:0046081 dUTP catabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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External links
PDB RCSB:3p48, PDBe:3p48, PDBj:3p48
PDBsum3p48
PubMed21548881
UniProtP33317|DUT_YEAST Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=DUT1)

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