Structure of PDB 1e2p Chain A

Receptor sequence
>1e2pA (length=305) Species: 10298 (Human alphaherpesvirus 1) [Search protein sequence]
MPTLLRVYIDGPHGMGKTTTTQLLRDDIVYVPEPMTYWRVLGASETIANI
YTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSP
PALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIV
LGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQCGGS
WREDWGQLSGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRL
RSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFA
REMGE
3D structure
PDB1e2p The Effect of Substrate Binding on the Conformation and Structural Stability of Herpes Simplex Virus Type 1 Thymidine Kinase
ChainA
Resolution2.5 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
Catalytic site (residue number reindexed from 1) K17 E33 D108 R109
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 CCV A H58 E83 W88 Q125 M128 R163 A168 Y172 H13 E33 W38 Q75 M78 R109 A114 Y118 MOAD: Ki=27uM
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:1e2p, PDBe:1e2p, PDBj:1e2p
PDBsum1e2p
PubMed11266595
UniProtP0DTH5|KITH_HHV11 Thymidine kinase (Gene Name=TK)

[Back to BioLiP]