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 | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006172 | biological_process | ADP 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 | 0046033 | biological_process | AMP metabolic process |
| A | 0046034 | biological_process | ATP metabolic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | PRO24 |
| A | GLY26 |
| A | ALA27 |
| A | GLY28 |
| A | LYS29 |
| A | GLY30 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvrQ |
| Chain | Residue | Details |
| A | PHE97-GLN108 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Region: {"description":"NMP"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 37 |
| Details | Region: {"description":"LID"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54819","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP6","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP6","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P54819","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | ARG187 | |
| A | ASP179 | |
| A | ARG143 | |
| A | ASP178 | |
| A | ARG176 | |
| A | LYS29 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | ARG143 | |
| A | ASP49 | |
| A | ASP167 | |
| A | LYS29 | |
