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3E2I

Crystal structure of Thymidine Kinase from S. aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004797molecular_functionthymidine kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006259biological_processDNA metabolic process
A0008270molecular_functionzinc ion binding
A0009157biological_processdeoxyribonucleoside monophosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046104biological_processthymidine metabolic process
A0046872molecular_functionmetal ion binding
A0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 200
ChainResidue
ACYS145
ACYS148
ACYS183
AHIS186

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
ALYS21
ASER22
AARG31
AHOH227
ASER16
AMSE17
APHE18
ASER19
AGLY20

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KEEL
ChainResidueDetails
ALYS196-LEU199

site_idPS00603
Number of Residues14
DetailsTK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GanEsYePrCRaHH
ChainResidueDetails
AGLY174-HIS187

224931

PDB entries from 2024-09-11

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