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4EAQ

Crystal structure of Thymidylate Kinase from Staphylococcus aureus in complex with 3'-Azido-3'-Deoxythymidine-5'-Monophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004798molecular_functionthymidylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006227biological_processdUDP biosynthetic process
A0006233biological_processdTDP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0006520biological_processamino acid metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016597molecular_functionamino acid binding
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0046940biological_processnucleoside monophosphate phosphorylation
B0004798molecular_functionthymidylate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006227biological_processdUDP biosynthetic process
B0006233biological_processdTDP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0006520biological_processamino acid metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016597molecular_functionamino acid binding
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATM A 301
ChainResidue
APHE-4
ATYR100
AGLN101
AHOH481
AGLU11
ALYS15
AARG36
AGLU37
APHE66
AARG70
AARG92
ASER97

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATM B 301
ChainResidue
BGLU11
BLYS15
BARG36
BGLU37
BARG48
BPHE66
BARG70
BARG92
BSER97
BTYR100
BGLN101
BHOH427

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. LCDRYidSSlAYQ
ChainResidueDetails
ALEU89-GLN101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00165
ChainResidueDetails
AGLY9
BGLY9

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PDB entries from 2024-11-06

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