6C9H
non-phosphorylated AMP-activated protein kinase bound to pharmacological activator R734
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004679 | molecular_function | AMP-activated protein kinase activity |
C | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006110 | biological_process | regulation of glycolytic process |
C | 0006468 | biological_process | protein phosphorylation |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0007165 | biological_process | signal transduction |
C | 0007283 | biological_process | spermatogenesis |
C | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
C | 0016020 | cellular_component | membrane |
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 | 0042149 | biological_process | cellular response to glucose starvation |
C | 0043531 | molecular_function | ADP binding |
C | 0043609 | biological_process | regulation of carbon utilization |
C | 0044877 | molecular_function | protein-containing complex binding |
C | 0045722 | biological_process | positive regulation of gluconeogenesis |
C | 0051170 | biological_process | import into nucleus |
C | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue R34 A 601 |
Chain | Residue |
A | VAL13 |
B | ASP108 |
B | ASN111 |
B | VAL113 |
A | LEU20 |
A | PHE29 |
A | LYS33 |
A | ILE48 |
A | ASN50 |
A | ASP90 |
B | ARG83 |
B | THR106 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue STU A 602 |
Chain | Residue |
A | LEU24 |
A | GLY25 |
A | VAL26 |
A | ALA45 |
A | LYS47 |
A | MET95 |
A | GLU96 |
A | TYR97 |
A | VAL98 |
A | GLY101 |
A | GLU102 |
A | GLU145 |
A | ASN146 |
A | LEU148 |
A | ASP159 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue AMP C 1101 |
Chain | Residue |
C | MET84 |
C | THR86 |
C | THR88 |
C | ASP89 |
C | PRO127 |
C | LEU128 |
C | VAL129 |
C | HIS150 |
C | ARG151 |
C | PRO153 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue AMP C 1102 |
Chain | Residue |
A | GLU364 |
C | ARG69 |
C | LYS169 |
C | ILE239 |
C | SER241 |
C | PHE243 |
C | ASP244 |
C | ARG268 |
C | VAL275 |
C | LEU276 |
C | VAL296 |
C | HIS297 |
C | ARG298 |
site_id | AC5 |
Number of Residues | 12 |
Details | binding site for residue AMP C 1103 |
Chain | Residue |
C | HIS150 |
C | THR199 |
C | ASN202 |
C | ALA204 |
C | VAL224 |
C | SER225 |
C | ALA226 |
C | PRO228 |
C | HIS297 |
C | SER313 |
C | SER315 |
C | ASP316 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 252 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"UniProtKB","id":"Q5EG47","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80386","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
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_FI16 |
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_FI17 |
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_FI18 |
Number of Residues | 21 |
Details | Motif: {"description":"AMPK pseudosubstrate"} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17452784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24352254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25412657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CFF","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |