7APU
Structure of Adenylate kinase from Escherichia coli in complex with two ADP molecules refined at 1.36 A resolution.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004017 | molecular_function | AMP kinase activity |
A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006172 | biological_process | ADP biosynthetic process |
A | 0009123 | biological_process | nucleoside monophosphate metabolic process |
A | 0009132 | biological_process | nucleoside diphosphate metabolic process |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0015951 | biological_process | purine ribonucleotide interconversion |
A | 0016208 | molecular_function | AMP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
A | 0044209 | biological_process | AMP salvage |
A | 0046083 | biological_process | adenine metabolic process |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004017 | molecular_function | AMP kinase activity |
B | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006172 | biological_process | ADP biosynthetic process |
B | 0009123 | biological_process | nucleoside monophosphate metabolic process |
B | 0009132 | biological_process | nucleoside diphosphate metabolic process |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0015951 | biological_process | purine ribonucleotide interconversion |
B | 0016208 | molecular_function | AMP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
B | 0044209 | biological_process | AMP salvage |
B | 0046083 | biological_process | adenine metabolic process |
B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00113 |
Number of Residues | 12 |
Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ |
Chain | Residue | Details |
A | PHE81-GLN92 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 58 |
Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8805521","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 74 |
Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8805521","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 26 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1548697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16302237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805185","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7937733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451239","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1548697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805185","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451239","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16302237","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1548697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16302237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805185","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451239","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |