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5NQ5

Mtb TMK crystal structure in complex with compound 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004798molecular_functiondTMP kinase activity
A0005524molecular_functionATP binding
A0005525molecular_functionGTP 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
A0042803molecular_functionprotein homodimerization activity
A0046044biological_processTMP metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 952 A 301
ChainResidue
ATYR39
ALEU52
AMET66
APHE70
AARG74
AASN100
ATYR103
AARG107
APRO210

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. ILDRYvaSNaAYS
ChainResidueDetails
AILE92-SER104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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