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2CCG

Crystal structure of His-tagged S. aureus thymidylate kinase complexed with thymidine monophosphate (TMP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004798molecular_functionthymidylate kinase activity
A0005524molecular_functionATP binding
A0006233biological_processdTDP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0046940biological_processnucleoside monophosphate phosphorylation
B0004798molecular_functionthymidylate kinase activity
B0005524molecular_functionATP binding
B0006233biological_processdTDP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TMP A1205
ChainResidue
AGLU11
ATYR100
AGLN101
AHOH2043
ALYS15
AARG36
AGLU37
APHE66
AARG70
AARG92
ASER96
ASER97

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TMP B1206
ChainResidue
BGLU11
BLYS15
BARG36
BPHE66
BARG70
BARG92
BSER97
BTYR100
BGLN101
BHOH2057

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ocp
ChainResidueDetails
ALYS86
AGLU37

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ocp
ChainResidueDetails
BLYS86
BGLU37

222624

PDB entries from 2024-07-17

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