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9R71

Crystal structure of E. coli Adenylate kinase E114A mutant in complex with inhibitor Ap5a.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004017molecular_functionAMP 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
A0016740molecular_functiontransferase activity
A0044209biological_processAMP salvage
A0046083biological_processadenine metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004017molecular_functionAMP 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
B0016740molecular_functiontransferase activity
B0044209biological_processAMP salvage
B0046083biological_processadenine metabolic process
B0046940biological_processnucleoside monophosphate phosphorylation
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 Residues58
DetailsRegion: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues74
DetailsRegion: {"description":"LID"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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