Structure of PDB 1e2k Chain A

Receptor sequence
>1e2kA (length=308) Species: 10299 (Human alphaherpesvirus 1 strain 17) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLVADDIVYVPEPMTYWRVLGASETIAN
IYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGP
PPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNI
VLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQCGG
SWREDWGQLSGTGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLA
KRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLAR
TFAREMGE
3D structure
PDB1e2k Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes Simplex Virus Type 1 Thymidine Kinase Interacting with (North)-Methanocarba-Thymidine
ChainA
Resolution1.7 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 E225
Catalytic site (residue number reindexed from 1) K17 E34 D109 R110 R167 E172
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 TMC A H58 E83 I97 Q125 M128 R163 A168 Y172 R222 H13 E34 I48 Q76 M79 R110 A115 Y119 R169 MOAD: Ki=11.4uM
PDBbind-CN: -logKd/Ki=4.94,Ki=11.4uM
Gene Ontology
Molecular Function
GO:0004797 thymidine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006230 TMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1e2k, PDBe:1e2k, PDBj:1e2k
PDBsum1e2k
PubMed10924157
UniProtP0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)

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