Structure of PDB 1osn Chain D

Receptor sequence
>1osnD (length=315) Species: 10335 (Human alphaherpesvirus 3) [Search protein sequence]
VKMGVLRIYLDGAYGIGKTTAAEEFLHHFAITPNRILLIGEPLSYWRNLA
GEDAICGIYGTQTRRLNGDVSPEDAQRLTAHFQSLFCSPHAIMHAKISAL
MDTSTEPYKIMLSDRHPIASTICFPLSRYLVGDMSPAALPGLLFTLPAEP
PGTNLVVCTVSLPSHLSRVTVNLPFVMVLRNVYIMLINTIIFLKTNNWHA
GWNTLSFCNDVFKQKLQKSECIKLREVPGIEDTLFAVLKLPELCGEFGNI
LPLWAWGMETLSNCLRSMSPFVLSLEQTPQHAAQELKTLLPQMTPANMSS
GAWNILKELVNAVQD
3D structure
PDB1osn Crystal structure of varicella zoster virus thymidine kinase
ChainD
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K25 E48 D129 R130
Catalytic site (residue number reindexed from 1) K18 E41 D114 R115
Enzyme Commision number 2.7.1.21: thymidine 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 ADP D G22 I23 G24 K25 T26 T27 R183 G15 I16 G17 K18 T19 T20 R168
BS02 BVP D Y21 E48 W53 I62 Y66 Q90 F93 R130 S135 F139 Y14 E41 W46 I55 Y59 Q83 F86 R115 S120 F124
Gene Ontology
Molecular Function
GO:0004797 thymidine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006230 TMP biosynthetic process
GO:0009157 deoxyribonucleoside monophosphate biosynthetic process
GO:0016310 phosphorylation
GO:0071897 DNA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1osn, PDBe:1osn, PDBj:1osn
PDBsum1osn
PubMed12686543
UniProtP0C0E6|KITH_VZVO Thymidine kinase (Gene Name=TK)

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