Structure of PDB 2we2 Chain A

Receptor sequence
>2we2A (length=248) Species: 10377 (Human herpesvirus 4 strain B95-8) [Search protein sequence]
CPHIRYAFQNDKLLLQQASVGRLTLVNKTTILLRPMKTTTVDLGLYARPP
EGHGLMLWGSTSRPVTSHVGIIDPDYTGELRLILQNQRRYNSTLRPSELK
IHLAAFRYATPQGPINHPQYPGSVGLDVSLPKDLALFPHQTVSVTLTVPP
PSIPHHRPTIFGRSGLAMQGILVKPCRWRRGGVDVSLTNFSDQTVFLNKY
RRFCQLVYLHKHHLTSFYSPHSDAGVLGPRSLFRWASCTFEEVPSLAM
3D structure
PDB2we2 The Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase is Essential for Catalysis.
ChainA
Resolution1.5 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 UMP A G73 I75 D76 Y79 R84 R171 S172 G70 I72 D73 Y76 R81 R163 S164
Gene Ontology
Molecular Function
GO:0004170 dUTP diphosphatase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009117 nucleotide metabolic process
GO:0046080 dUTP metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2we2, PDBe:2we2, PDBj:2we2
PDBsum2we2
PubMed19586911
UniProtP03195|DUT_EBVB9 Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=DUT)

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