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8RJ4

E. coli adenylate kinase in complex with two ADP molecules and Mg2+ as a result of enzymatic AP4A hydrolysis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004017molecular_functionadenylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006172biological_processADP biosynthetic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009132biological_processnucleoside diphosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0015951biological_processpurine ribonucleotide interconversion
A0016208molecular_functionAMP binding
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0000287molecular_functionmagnesium ion binding
B0004017molecular_functionadenylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006172biological_processADP biosynthetic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009132biological_processnucleoside diphosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0015951biological_processpurine ribonucleotide interconversion
B0016208molecular_functionAMP binding
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
C0000287molecular_functionmagnesium ion binding
C0004017molecular_functionadenylate kinase activity
C0004550molecular_functionnucleoside diphosphate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006172biological_processADP biosynthetic process
C0009123biological_processnucleoside monophosphate metabolic process
C0009132biological_processnucleoside diphosphate metabolic process
C0009165biological_processnucleotide biosynthetic process
C0015951biological_processpurine ribonucleotide interconversion
C0016208molecular_functionAMP binding
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0044209biological_processAMP salvage
C0046940biological_processnucleoside monophosphate phosphorylation
C0050145molecular_functionnucleoside monophosphate kinase activity
D0000287molecular_functionmagnesium ion binding
D0004017molecular_functionadenylate kinase activity
D0004550molecular_functionnucleoside diphosphate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006172biological_processADP biosynthetic process
D0009123biological_processnucleoside monophosphate metabolic process
D0009132biological_processnucleoside diphosphate metabolic process
D0009165biological_processnucleotide biosynthetic process
D0015951biological_processpurine ribonucleotide interconversion
D0016208molecular_functionAMP binding
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0044209biological_processAMP salvage
D0046940biological_processnucleoside monophosphate phosphorylation
D0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ
ChainResidueDetails
APHE81-GLN92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733, ECO:0000269|PubMed:8451239
ChainResidueDetails
AGLY10
BTHR31
BARG36
BLYS57
BGLN92
BARG123
BARG156
BLYS200
CGLY10
CTHR31
CARG36
ATHR31
CLYS57
CGLN92
CARG123
CARG156
CLYS200
DGLY10
DTHR31
DARG36
DLYS57
DGLN92
AARG36
DARG123
DARG156
DLYS200
ALYS57
AGLN92
AARG123
AARG156
ALYS200
BGLY10

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239
ChainResidueDetails
AGLY85
AARG167
BGLY85
BARG167
CGLY85
CARG167
DGLY85
DARG167

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16302237
ChainResidueDetails
AARG119
BARG119
CARG119
DARG119

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239
ChainResidueDetails
AVAL132
BVAL132
CVAL132
DVAL132

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS192
BLYS192
CLYS192
DLYS192

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PDB entries from 2024-10-09

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