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5NR7

Mtb TMK crystal structure in complex with compound 43

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004798molecular_functionthymidylate 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
A0042803molecular_functionprotein homodimerization activity
A0046044biological_processTMP metabolic process
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
B0000287molecular_functionmagnesium ion binding
B0004798molecular_functionthymidylate kinase activity
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006227biological_processdUDP biosynthetic process
B0006233biological_processdTDP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0042803molecular_functionprotein homodimerization activity
B0046044biological_processTMP metabolic process
B0046872molecular_functionmetal ion binding
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue YUI A 301
ChainResidue
AASP9
ATYR103
AHOH419
APHE36
APRO37
ALEU52
AHIS53
APHE70
AARG74
AARG95
AASN100

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AGLY10
AALA11
AGLY12
ALYS13
AHOH425

site_idAC3
Number of Residues9
Detailsbinding site for residue YUI B 301
ChainResidue
BASP9
BPHE36
BPRO37
BLEU52
BPHE70
BARG74
BARG95
BASN100
BTYR103

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 302
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13

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 Residues22
DetailsBINDING:
ChainResidueDetails
ATYR39
APHE70
AARG74
AARG95
AASN100
ATYR103
AASP163
ATYR165
AGLU166
BGLY7
BASP9
BTYR39
BPHE70
BARG74
BARG95
BASN100
BTYR103
BASP163
BTYR165
BGLU166
AGLY7
AASP9

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255
ChainResidueDetails
AARG153
BARG153

221051

PDB entries from 2024-06-12

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