7JHG
Cryo-EM structure of ATP-bound fully inactive AMPK in complex with Dorsomorphin (Compound C) and Fab-nanobody
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004679 | molecular_function | AMP-activated protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005654 | cellular_component | nucleoplasm |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0006110 | biological_process | regulation of glycolytic process |
| G | 0006468 | biological_process | protein phosphorylation |
| G | 0006633 | biological_process | fatty acid biosynthetic process |
| G | 0007165 | biological_process | signal transduction |
| G | 0007283 | biological_process | spermatogenesis |
| G | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
| G | 0010628 | biological_process | positive regulation of gene expression |
| G | 0016020 | cellular_component | membrane |
| G | 0016208 | molecular_function | AMP binding |
| G | 0019887 | molecular_function | protein kinase regulator activity |
| G | 0019901 | molecular_function | protein kinase binding |
| G | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
| G | 0031669 | biological_process | cellular response to nutrient levels |
| G | 0043531 | molecular_function | ADP binding |
| G | 0045860 | biological_process | positive regulation of protein kinase activity |
| G | 0051170 | biological_process | import into nucleus |
| M | 0055085 | biological_process | transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK |
| Chain | Residue | Details |
| A | LEU24-LYS47 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL |
| Chain | Residue | Details |
| A | VAL137-LEU149 |
| site_id | PS01037 |
| Number of Residues | 18 |
| Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
| Chain | Residue | Details |
| M | PRO107-ASN124 |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
| Chain | Residue | Details |
| L | TYR193-HIS199 | |
| H | TYR210-HIS216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P80385 |
| Chain | Residue | Details |
| G | ARG152 | |
| G | LYS170 | |
| G | SER242 | |
| G | ARG269 | |
| G | LEU277 | |
| G | ARG70 | |
| G | MET85 | |
| G | VAL130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF |
| Chain | Residue | Details |
| G | ALA205 | |
| G | SER226 | |
| G | HIS298 | |
| G | SER314 | |
| G | HIS151 | |
| G | THR200 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 |
| Chain | Residue | Details |
| G | SER261 | |
| G | SER270 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385 |
| Chain | Residue | Details |
| G | THR263 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | HIS533 | |
| B | SER184 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR346 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER347 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P54645 |
| Chain | Residue | Details |
| A | SER351 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645 |
| Chain | Residue | Details |
| A | THR359 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR373 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54645 |
| Chain | Residue | Details |
| A | SER388 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER458 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | GLY531 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | ILE535 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | CYS541 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
