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2QQE

Thymidine Kinase from Thermotoga Maritima in complex with Thymidine

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
A0042802molecular_functionidentical protein binding
A0046104biological_processthymidine metabolic process
A0046872molecular_functionmetal ion binding
A0071897biological_processDNA biosynthetic process
B0004797molecular_functionthymidine kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006259biological_processDNA metabolic process
B0008270molecular_functionzinc ion binding
B0009157biological_processdeoxyribonucleoside monophosphate biosynthetic process
B0016301molecular_functionkinase activity
B0042802molecular_functionidentical protein binding
B0046104biological_processthymidine metabolic process
B0046872molecular_functionmetal ion binding
B0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS140
ACYS143
ACYS173
ACYS176

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS140
BCYS143
BCYS173
BCYS176

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE THM A 501
ChainResidue
AGLN86
APHE87
ALEU111
ATHR114
AHIS115
ATHR151
AGLU160
AILE161
AASP162
AVAL163
AGLY164
ATYR169
AGLU84

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE THM B 502
ChainResidue
BGLU84
BGLN86
BPHE87
BLEU111
BTHR114
BHIS115
BPHE120
BILE161
BASP162
BVAL163
BGLY164
BTYR169

Functional Information from PROSITE/UniProt
site_idPS00603
Number of Residues14
DetailsTK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GgqEkYiAvCRdCY
ChainResidueDetails
AGLY164-TYR177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
AGLU84
BGLU84

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AGLY10
BGLY10
BHIS53
BHIS115
BCYS140
BCYS143
BILE161
BTYR169
BCYS173
BCYS176
AHIS53
AHIS115
ACYS140
ACYS143
AILE161
ATYR169
ACYS173
ACYS176

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP83
BASP83

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PDB entries from 2024-07-24

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