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5H5B

Citrate ion bound crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004798molecular_functiondTMP kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006227biological_processdUDP biosynthetic process
A0006233biological_processdTDP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
B0000166molecular_functionnucleotide binding
B0004798molecular_functiondTMP kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006227biological_processdUDP biosynthetic process
B0006233biological_processdTDP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue FLC B 201
ChainResidue
BASP9
BGLY10
BSER11
BGLY12
BLYS13
BTHR14
BTHR15
BARG145

site_idAC2
Number of Residues8
Detailsbinding site for residue FLC A 201
ChainResidue
AGLY10
ASER11
AGLY12
ALYS13
ATHR14
ATHR15
AARG145
AASP9

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. ILDRFvlSTiAYQ
ChainResidueDetails
BILE87-GLN99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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