Structure of PDB 3zf5 Chain A

Receptor sequence
>3zf5A (length=169) Species: 53369 (Dubowvirus dv80alpha) [Search protein sequence]
TNTLQVKLLSKNARMPERNHKTDAGYDIFSAETVVLEPQEKAVIKTDVAV
SIPEGYVGLLTSRSGVSSKTHLVIETGKIDAGFHGNLGINIKNDHEDDKM
QTIFLRNIDNEKIFEKERHLYKLGSYRIEKGERIAQLVIVPIWTPELKQV
EEFESVSERGEKGFGSSGV
3D structure
PDB3zf5 Phage Dutpases Control Transfer of Virulence Genes by a Proto-Oncogenic G Protein-Like Mechanism.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) A25 R64 G66 L73 D81
Catalytic site (residue number reindexed from 1) A24 R63 G65 L72 D80
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 G78 I80 D81 F84 G89 G77 I79 D80 F83 G88
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:0046081 dUTP catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3zf5, PDBe:3zf5, PDBj:3zf5
PDBsum3zf5
PubMed23333307
UniProtA4ZF98

[Back to BioLiP]