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2VTK

THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE 1 IN COMPLEX WITH ADP AND DEOXYTHYMIDINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004797molecular_functionthymidine kinase activity
A0005524molecular_functionATP binding
A0006230biological_processTMP biosynthetic process
A0009157biological_processdeoxyribonucleoside monophosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP A 400
ChainResidue
AGLY59
AGLN331
AHOH615
AMET60
AGLY61
ALYS62
ATHR63
ATHR64
AARG216
AARG220
AARG222

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE THM A 500
ChainResidue
AGLU83
AILE100
ATYR101
AGLN125
AALA168
AARG222
AGLU225
AHOH606
AHOH615
AHOH616

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04029
ChainResidueDetails
AGLU83

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04029
ChainResidueDetails
AGLY56
ATYR101
AGLN125
AARG216
AARG222

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kim
ChainResidueDetails
AGLU83
AARG222
AGLY59
AARG163

site_idMCSA1
Number of Residues7
DetailsM-CSA 588
ChainResidueDetails
ALYS62electrostatic stabiliser, polar interaction
AGLU83proton acceptor, proton donor
AASP162metal ligand
AARG163electrostatic stabiliser, polar interaction
AARG220electrostatic stabiliser, polar interaction
AARG222electrostatic stabiliser, polar interaction
AGLU225electrostatic stabiliser, polar interaction

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PDB entries from 2024-09-04

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