4EAG
Co-crystal structure of an chimeric AMPK core with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004679 | molecular_function | AMP-activated protein kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0010628 | biological_process | positive regulation of gene expression |
| C | 0016208 | molecular_function | AMP binding |
| C | 0019887 | molecular_function | protein kinase regulator activity |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
| C | 0031669 | biological_process | cellular response to nutrient levels |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0043531 | molecular_function | ADP binding |
| C | 0044877 | molecular_function | protein-containing complex binding |
| C | 0051170 | biological_process | import into nucleus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP C 401 |
| Chain | Residue |
| C | MET84 |
| C | ILE149 |
| C | HIS150 |
| C | ARG151 |
| C | PRO153 |
| C | SER225 |
| C | PHE243 |
| C | HOH509 |
| C | HOH539 |
| C | THR86 |
| C | ILE87 |
| C | THR88 |
| C | ASP89 |
| C | GLN122 |
| C | PRO127 |
| C | LEU128 |
| C | VAL129 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP C 402 |
| Chain | Residue |
| C | HIS150 |
| C | THR199 |
| C | ALA204 |
| C | VAL224 |
| C | SER225 |
| C | ALA226 |
| C | PRO228 |
| C | HIS297 |
| C | ARG298 |
| C | SER313 |
| C | LEU314 |
| C | SER315 |
| C | ASP316 |
| C | HOH515 |
| C | HOH538 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TAM C 403 |
| Chain | Residue |
| C | VAL68 |
| C | ARG69 |
| C | ARG151 |
| C | THR167 |
| C | LYS169 |
| C | ARG170 |
| C | HIS297 |
| C | HOH503 |
| C | HOH521 |
| C | HOH527 |
| C | HOH536 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 |
| Chain | Residue | Details |
| C | ARG69 | |
| C | MET84 | |
| C | VAL129 | |
| C | ARG151 | |
| C | LYS169 | |
| C | SER241 | |
| C | ARG268 | |
| C | LEU276 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L |
| Chain | Residue | Details |
| C | HIS150 | |
| C | THR199 | |
| C | ALA204 | |
| C | SER225 | |
| C | HIS297 | |
| C | SER313 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 |
| Chain | Residue | Details |
| C | SER260 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 |
| Chain | Residue | Details |
| C | THR262 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634 |
| Chain | Residue | Details |
| C | SER269 |
