Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 219 |
| Chain | Residue |
| A | CYS130 |
| A | CYS133 |
| A | CYS150 |
| A | CYS153 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE AP5 A 218 |
| Chain | Residue |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | PHE35 |
| A | ARG36 |
| A | MET53 |
| A | ASP57 |
| A | VAL59 |
| A | THR64 |
| A | GLY85 |
| A | ARG88 |
| A | GLN92 |
| A | ARG123 |
| A | LEU124 |
| A | ARG127 |
| A | TYR137 |
| A | HIS138 |
| A | HIS142 |
| A | ARG160 |
| A | ARG171 |
| A | GLN199 |
| A | MET201 |
| A | HOH300 |
| A | HOH301 |
| A | HOH306 |
| A | HOH309 |
| A | HOH311 |
| A | HOH352 |
| A | HOH355 |
| A | HOH426 |
| A | HOH532 |
| A | PRO9 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvaQ |
| Chain | Residue | Details |
| A | PHE81-GLN92 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 37 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9715904","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | LYS13 | |
| A | ARG127 | |
| A | ARG171 | |
| A | ARG160 | |
| A | ASP162 | |
| A | ASP163 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 290 |
| Chain | Residue | Details |
| A | LYS13 | electrostatic stabiliser |
| A | ARG88 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG127 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG160 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG171 | electrostatic stabiliser |
