2V8Q
Crystal structure of the regulatory fragment of mammalian AMPK in complexes with AMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004679 | molecular_function | AMP-activated protein kinase activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004679 | molecular_function | AMP-activated protein kinase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006110 | biological_process | regulation of glycolytic process |
E | 0006629 | biological_process | lipid metabolic process |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0016208 | molecular_function | AMP binding |
E | 0019887 | molecular_function | protein kinase regulator activity |
E | 0019901 | molecular_function | protein kinase binding |
E | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
E | 0031669 | biological_process | cellular response to nutrient levels |
E | 0032991 | cellular_component | protein-containing complex |
E | 0042149 | biological_process | cellular response to glucose starvation |
E | 0043531 | molecular_function | ADP binding |
E | 0043609 | biological_process | regulation of carbon utilization |
E | 0044877 | molecular_function | protein-containing complex binding |
E | 0045722 | biological_process | positive regulation of gluconeogenesis |
E | 0051170 | biological_process | import into nucleus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AMP E1327 |
Chain | Residue |
E | ARG69 |
E | LEU276 |
E | VAL296 |
E | HIS297 |
E | ARG298 |
E | HOH2283 |
E | LYS169 |
E | ILE239 |
E | SER241 |
E | PHE243 |
E | ASP244 |
E | ARG268 |
E | PHE272 |
E | VAL275 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AMP E1328 |
Chain | Residue |
E | MET84 |
E | THR86 |
E | THR88 |
E | ASP89 |
E | PRO127 |
E | LEU128 |
E | VAL129 |
E | ILE149 |
E | HIS150 |
E | ARG151 |
E | PRO153 |
E | HOH2284 |
E | HOH2286 |
E | HOH2287 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AMP E1329 |
Chain | Residue |
A | ARG457 |
E | HIS150 |
E | THR199 |
E | ASN202 |
E | ILE203 |
E | ALA204 |
E | VAL224 |
E | SER225 |
E | ALA226 |
E | HIS297 |
E | ILE311 |
E | SER313 |
E | SER315 |
E | ASP316 |
E | HOH2238 |
E | HOH2289 |
E | HOH2290 |
E | HOH2291 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 62 |
Details | Domain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 62 |
Details | Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | Motif: {"description":"AMPK pseudosubstrate"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21399626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y8L","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |