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1N5L

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE CRYSTALLIZED IN SODIUM MALONATE, AFTER CATALYSIS IN THE CRYSTAL (2.3 A RESOLUTION)

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
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004798molecular_functiondTMP 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
B0016740molecular_functiontransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046044biological_processTMP metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 215
ChainResidue
BASP9
BGLU166
BTYD216
BHOH469
BHOH502

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 412
ChainResidue
AARG122
AARG127
BASN111

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 413
ChainResidue
AALA11
AGLY12
ALYS13
AGLY10

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TMP A 409
ChainResidue
APRO37
ATYR39
APHE70
AARG74
AARG95
AASN100
ATYR103
ATYR165
AHOH434
AHOH492

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE TYD B 216
ChainResidue
BASP9
BPHE36
BPRO37
BTYR39
BLEU52
BPHE70
BARG74
BARG95
BSER99
BASN100
BTYR103
BTYR165
BMG215
BHOH415
BHOH427
BHOH469
BHOH502

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DPO B 414
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BARG14
BTHR15
BHOH502

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 Residues34
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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