Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RJ9

E. coli adenylate kinase Asp84Ala variant in complex with two ADP molecules 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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
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
ATHR31
AARG36
ALYS57
AGLN92
AARG123
AARG156
ALYS200
BGLY10

site_idSWS_FT_FI2
Number of Residues4
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

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16302237
ChainResidueDetails
AARG119
BARG119

site_idSWS_FT_FI4
Number of Residues2
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

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS192
BLYS192

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon