Structure of PDB 2vp6 Chain F

Receptor sequence

>2vp6F (length=192) Species: 7227 (Drosophila melanogaster)

TKYAEGTQPFTVLIEGNIGSGKTTYLNHFEKYKNDICLLTEPVEKWRNVN
GVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKKLKIMERSIFSAR
YCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHVQADLIIYLRTSPEVAY
ERIRQRARSEESCVPLKYLQELHELHEDWLIHQCKVLVLDAD

3D structure

• PDB: 2vp6 Structural Studies of Nucleoside Analog and Feedback Inhibitor Binding to Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase.
• Chain: F
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E52 R105
• Catalytic site (residue number reindexed from 1): E41 R94
• Enzyme Commision number: 2.7.1.145: deoxynucleoside kinase.

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	5FU	F	E52 W57 Y70 F80 Q81 R105 A110 F114	E41 W46 Y59 F69 Q70 R94 A99 F103

Gene Ontology

Molecular Function

• GO:0004136 deoxyadenosine kinase activity
• GO:0004137 deoxycytidine kinase activity
• GO:0004138 deoxyguanosine kinase activity
• GO:0004797 thymidine kinase activity
• GO:0004849 uridine kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0019136 deoxynucleoside kinase activity
• GO:0043771 cytidine kinase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0006170 dAMP biosynthetic process
• GO:0006222 UMP biosynthetic process
• GO:0009157 deoxyribonucleoside monophosphate biosynthetic process
• GO:0009224 CMP biosynthetic process
• GO:0016310 phosphorylation
• GO:0043174 nucleoside salvage
• GO:0071897 DNA biosynthetic process
• GO:1901293 nucleoside phosphate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005739 mitochondrion

External links

• PDB: RCSB:2vp6, PDBe:2vp6, PDBj:2vp6
• PDBsum: 2vp6
• PubMed: 18384378
• UniProt: Q9XZT6|DNK_DROME Deoxynucleoside kinase (Gene Name=dnk)