2V9J
Crystal structure of the regulatory fragment of mammalian AMPK in complexes with Mg.ATP-AMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004679 | molecular_function | AMP-activated protein kinase activity |
E | 0004672 | molecular_function | protein kinase activity |
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 | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0010628 | biological_process | positive regulation of gene expression |
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 | 0043531 | molecular_function | ADP binding |
E | 0044877 | molecular_function | protein-containing complex binding |
E | 0051170 | biological_process | import into nucleus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP E1327 |
Chain | Residue |
E | ARG69 |
E | VAL275 |
E | LEU276 |
E | VAL296 |
E | HIS297 |
E | ARG298 |
E | LEU314 |
E | MG1330 |
E | HOH2074 |
E | HOH2075 |
E | HOH2076 |
E | ARG151 |
E | HOH2077 |
E | HOH2078 |
E | LYS169 |
E | ILE239 |
E | SER241 |
E | PHE243 |
E | ASP244 |
E | ARG268 |
E | PHE272 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ATP E1328 |
Chain | Residue |
E | MET84 |
E | THR86 |
E | ILE87 |
E | THR88 |
E | ASP89 |
E | PRO127 |
E | LEU128 |
E | VAL129 |
E | ILE149 |
E | HIS150 |
E | ARG151 |
E | PRO153 |
E | SER225 |
E | LYS242 |
E | MG1331 |
E | HOH2078 |
E | HOH2079 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AMP E1329 |
Chain | Residue |
A | ARG457 |
E | HIS150 |
E | THR199 |
E | ILE203 |
E | ALA204 |
E | VAL224 |
E | SER225 |
E | ALA226 |
E | HIS297 |
E | ILE311 |
E | SER313 |
E | SER315 |
E | ASP316 |
E | HOH2079 |
E | HOH2080 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E1330 |
Chain | Residue |
E | LYS169 |
E | ATP1327 |
E | HOH2074 |
E | HOH2077 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG E1331 |
Chain | Residue |
E | ILE87 |
E | ATP1328 |
E | HOH2078 |
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 |
E | ARG69 | |
E | MET84 | |
E | VAL129 | |
E | ARG151 | |
E | LYS169 | |
E | SER241 | |
E | ARG268 | |
E | 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 |
E | HIS150 | |
E | THR199 | |
E | ALA204 | |
E | SER225 | |
E | HIS297 | |
E | SER313 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
E | SER260 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 |
Chain | Residue | Details |
E | THR262 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634 |
Chain | Residue | Details |
E | SER269 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12764152, ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | ASP496 |