Structure of PDB 1qhi Chain B

Receptor sequence
>1qhiB (length=304) Species: 10299 (Human alphaherpesvirus 1 strain 17) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLVALDIVYVPEPMTYWRVLGASETIAN
IYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAPP
ALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVL
GALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQCGGSW
REDWGQLAGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLR
SMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAR
EMGE
3D structure
PDB1qhi Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir.
ChainB
Resolution1.9 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 E34 D107 R108 R165 R167 E170
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 BPG B E83 W88 I100 Y101 Q125 M128 Y132 R163 A168 Y172 R176 R222 E34 W39 I51 Y52 Q76 M79 Y83 R108 A113 Y117 R121 R167
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:1qhi, PDBe:1qhi, PDBj:1qhi
PDBsum1qhi
PubMed9989588
UniProtP0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)

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