Structure of PDB 2vtk Chain A

Receptor sequence

>2vtkA (length=313) Species: 10304 (Human alphaherpesvirus 1 strain F)

MPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASE
TIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGG
EAGSPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTL
PGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRY
LQCGGSWREDWGQLSGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALD
VLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICD
LARTFAREMGEAN

3D structure

• PDB: 2vtk The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.
• Chain: A
• Resolution: 2.8 Å

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 K219 R220 R222 Q331 P333	G14 M15 G16 K17 T18 T19 R168 K171 R172 R174 Q268 P270
BS02	THM	A	H58 E83 I97 Y101 Q125 M128 A168 Y172 R222 E225	H13 E38 I52 Y56 Q80 M83 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

External links

• PDB: RCSB:2vtk, PDBe:2vtk, PDBj:2vtk
• PDBsum: 2vtk
• PubMed: 9336833
• UniProt: P0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)