Structure of PDB 1e2k Chain B

Receptor sequence
>1e2kB (length=316) Species: 10299 (Human alphaherpesvirus 1 strain 17) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASE
TIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGG
EAHAPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTL
PGTNIVLGALPEDRHIDRLAKRERLDLAMLAAIRRVYGLLANTVRYLQCG
GSWREDWGQLSGTAVPQSNAGPRPHIGDTLFTLFRAPELLAPNGDLYNVF
AWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSI
PTICDLARTFAREMGE
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
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K62 E83 D162 R163 R220 E225
Catalytic site (residue number reindexed from 1) K17 E38 D114 R115 R172 E173
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 B H58 I97 Q125 M128 R163 A168 Y172 E225 H13 I52 Q80 M83 R115 A120 Y124 E173 MOAD: Ki=11.4uM
Gene Ontology
Molecular Function
GO:0004797 thymidine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006230 TMP biosynthetic process

View graph for
Molecular Function

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

[Back to BioLiP]