4EAI
Co-crystal structure of an AMPK core with AMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004679 | molecular_function | AMP-activated protein kinase activity |
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 | 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 | 15 |
Details | BINDING SITE FOR RESIDUE AMP C 401 |
Chain | Residue |
C | ARG69 |
C | VAL275 |
C | LEU276 |
C | VAL296 |
C | HIS297 |
C | ARG298 |
C | HOH558 |
C | LYS169 |
C | ILE239 |
C | SER241 |
C | PHE243 |
C | ASP244 |
C | ARG268 |
C | PHE272 |
C | GLY274 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AMP C 402 |
Chain | Residue |
C | MET84 |
C | THR86 |
C | THR88 |
C | ASP89 |
C | LYS126 |
C | PRO127 |
C | LEU128 |
C | VAL129 |
C | ILE149 |
C | HIS150 |
C | ARG151 |
C | PRO153 |
C | HOH508 |
C | HOH528 |
C | HOH536 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AMP C 403 |
Chain | Residue |
C | HIS150 |
C | THR199 |
C | ILE203 |
C | ALA204 |
C | VAL224 |
C | SER225 |
C | ALA226 |
C | HIS297 |
C | SER313 |
C | SER315 |
C | ASP316 |
C | HOH516 |
C | HOH518 |
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 |