Structure of PDB 1vtk Chain A

Receptor sequence
>1vtkA (length=313) Species: 10304 (Human alphaherpesvirus 1 strain F) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASE
TIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGG
EAGSPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTL
PGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRY
LQCGGSWREDWGQLSGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALD
VLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICD
LARTFAREMGEAN
3D structure
PDB1vtk The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.
ChainA
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K62 E83 D162 R163 R220 R222 E225
Catalytic site (residue number reindexed from 1) K17 E38 D114 R115 R172 R174 E177
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 A G59 M60 G61 K62 T63 T64 R216 R220 Q331 P333 G14 M15 G16 K17 T18 T19 R168 R172 Q268 P270
BS02 TMP A H58 E83 Y101 Q125 M128 R163 A168 Y172 R222 E225 H13 E38 Y56 Q80 M83 R115 A120 Y124 R174 E177
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:1vtk, PDBe:1vtk, PDBj:1vtk
PDBsum1vtk
PubMed9336833
UniProtP0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)

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