Structure of PDB 1e2l Chain A

Receptor sequence
>1e2lA (length=304) Species: 10299 (Human alphaherpesvirus 1 strain 17) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLDIVYVPEPMTYWRVLGASETIANIFT
TQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSPPP
ALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVL
GALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQCGGSW
REDWGQLSGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLR
SMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAR
EMGE
3D structure
PDB1e2l 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
Resolution2.4 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
Catalytic site (residue number reindexed from 1) K17 E31 D107 R108
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 I97 Q125 M128 R163 Y172 R222 H13 I45 Q73 M76 R108 Y117 R167 MOAD: Ki=51.5uM
PDBbind-CN: -logKd/Ki=4.29,Ki=51.5uM
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:1e2l, PDBe:1e2l, PDBj:1e2l
PDBsum1e2l
PubMed10924157
UniProtP0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)

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