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3LD9

Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution

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
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase 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
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0046940biological_processnucleoside monophosphate phosphorylation
C0004798molecular_functionthymidylate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006227biological_processdUDP biosynthetic process
C0006233biological_processdTDP biosynthetic process
C0006235biological_processdTTP biosynthetic process
C0009165biological_processnucleotide biosynthetic process
C0016301molecular_functionkinase activity
C0046940biological_processnucleoside monophosphate phosphorylation
D0004798molecular_functionthymidylate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006227biological_processdUDP biosynthetic process
D0006233biological_processdTDP biosynthetic process
D0006235biological_processdTTP biosynthetic process
D0009165biological_processnucleotide biosynthetic process
D0016301molecular_functionkinase activity
D0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AILE8
AASP9
AGLY10
ASER11
AGLY12
ALYS13
ATHR14
AHOH256

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 300
ChainResidue
BASP9
BGLY10
BSER11
BGLY12
BLYS13
BTHR14
BHOH260
BHOH275
BILE8

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BGLU38
BARG71
BARG93
BPHE94
BTHR98
BHOH204

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 300
ChainResidue
CILE8
CGLY10
CSER11
CGLY12
CLYS13
CTHR14

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 300
ChainResidue
DASP9
DGLY10
DSER11
DGLY12
DLYS13
DTHR14
DHOH210
DHOH237

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D 301
ChainResidue
DGLU38
DPHE67
DARG71
DPHE94
DTHR98
DHOH282

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. ICDRFidSTiAYQ
ChainResidueDetails
AILE90-GLN102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00165
ChainResidueDetails
AGLY7
BGLY7
CGLY7
DGLY7

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PDB entries from 2024-06-12

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