Structure of PDB 2ol1 Chain C

Receptor sequence
>2ol1C (length=125) Species: 10245 (Vaccinia virus) [Search protein sequence]
NSPVRFVKETNRAKSPTRQSPGAAGYDLYSAYDYTIPPGERQLIKTDISM
SMPKFCYGRIAPRSGLSLKGIDIGGGVIDEDYRGNIGVILINNGKCTFNV
NTGDRIAQLIYQRIYYPELEEVQSL
3D structure
PDB2ol1 Structures of vaccinia virus dUTPase and its nucleotide complexes.
ChainC
Resolution1.8 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) A30 R69 G71 I77 D85
Catalytic site (residue number reindexed from 1) A24 R63 G65 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 UMP C R69 S70 R63 S64
BS02 UMP C G82 V83 I84 D85 Y88 G93 G76 V77 I78 D79 Y82 G87
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:0009117 nucleotide metabolic process
GO:0046081 dUTP catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2ol1, PDBe:2ol1, PDBj:2ol1
PDBsum2ol1
PubMed17452782
UniProtP17374|DUT_VACCW Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=OPG046)

[Back to BioLiP]