5EZV
X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid)
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 |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0007165 | biological_process | signal transduction |
B | 0019901 | molecular_function | protein kinase binding |
B | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
B | 0031669 | biological_process | cellular response to nutrient levels |
B | 0032991 | cellular_component | protein-containing complex |
B | 0035878 | biological_process | nail development |
B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004679 | molecular_function | AMP-activated protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006629 | biological_process | lipid metabolic process |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0007165 | biological_process | signal transduction |
D | 0019901 | molecular_function | protein kinase binding |
D | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
D | 0031669 | biological_process | cellular response to nutrient levels |
D | 0032991 | cellular_component | protein-containing complex |
D | 0035878 | biological_process | nail development |
D | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004679 | molecular_function | AMP-activated protein kinase activity |
E | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006110 | biological_process | regulation of glycolytic process |
E | 0006468 | biological_process | protein phosphorylation |
E | 0006629 | biological_process | lipid metabolic process |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0007165 | biological_process | signal transduction |
E | 0007283 | biological_process | spermatogenesis |
E | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
E | 0016020 | cellular_component | membrane |
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 | 0042149 | biological_process | cellular response to glucose starvation |
E | 0043531 | molecular_function | ADP binding |
E | 0043609 | biological_process | regulation of carbon utilization |
E | 0044877 | molecular_function | protein-containing complex binding |
E | 0045722 | biological_process | positive regulation of gluconeogenesis |
E | 0051170 | biological_process | import into nucleus |
E | 0051726 | biological_process | regulation of cell cycle |
F | 0000166 | molecular_function | nucleotide binding |
F | 0004679 | molecular_function | AMP-activated protein kinase activity |
F | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005634 | cellular_component | nucleus |
F | 0005654 | cellular_component | nucleoplasm |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0006110 | biological_process | regulation of glycolytic process |
F | 0006468 | biological_process | protein phosphorylation |
F | 0006629 | biological_process | lipid metabolic process |
F | 0006631 | biological_process | fatty acid metabolic process |
F | 0006633 | biological_process | fatty acid biosynthetic process |
F | 0007165 | biological_process | signal transduction |
F | 0007283 | biological_process | spermatogenesis |
F | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
F | 0016020 | cellular_component | membrane |
F | 0016208 | molecular_function | AMP binding |
F | 0019887 | molecular_function | protein kinase regulator activity |
F | 0019901 | molecular_function | protein kinase binding |
F | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
F | 0031669 | biological_process | cellular response to nutrient levels |
F | 0032991 | cellular_component | protein-containing complex |
F | 0042149 | biological_process | cellular response to glucose starvation |
F | 0043531 | molecular_function | ADP binding |
F | 0043609 | biological_process | regulation of carbon utilization |
F | 0044877 | molecular_function | protein-containing complex binding |
F | 0045722 | biological_process | positive regulation of gluconeogenesis |
F | 0051170 | biological_process | import into nucleus |
F | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue STU A 601 |
Chain | Residue |
A | LEU22 |
A | VAL96 |
A | GLU100 |
A | GLU143 |
A | ASN144 |
A | LEU146 |
A | GLY23 |
A | VAL24 |
A | GLY25 |
A | VAL30 |
A | ALA43 |
A | MET93 |
A | GLU94 |
A | TYR95 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue C1V A 602 |
Chain | Residue |
A | LEU18 |
A | GLY19 |
A | LYS29 |
A | LYS31 |
A | ILE46 |
A | ASP88 |
B | ARG83 |
B | THR106 |
B | SEP108 |
B | VAL113 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue STU C 601 |
Chain | Residue |
C | LEU22 |
C | GLY23 |
C | VAL24 |
C | GLY25 |
C | VAL30 |
C | ALA43 |
C | GLU94 |
C | TYR95 |
C | VAL96 |
C | GLU100 |
C | GLU143 |
C | ASN144 |
C | LEU146 |
C | ASP157 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue C1V C 602 |
Chain | Residue |
C | VAL11 |
C | LEU18 |
C | GLY19 |
C | LYS29 |
C | LYS31 |
C | ILE46 |
C | ASN48 |
C | ASP88 |
D | ARG83 |
D | ARG107 |
D | SEP108 |
D | VAL113 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue C2Z E 401 |
Chain | Residue |
E | HIS151 |
E | ARG152 |
E | SER226 |
E | HIS298 |
E | ARG299 |
E | SER314 |
E | SER316 |
E | C2Z402 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue C2Z E 402 |
Chain | Residue |
E | ARG70 |
E | THR87 |
E | THR89 |
E | HIS151 |
E | SER226 |
E | SER242 |
E | LYS243 |
E | PHE244 |
E | ARG299 |
E | C2Z401 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue C2Z F 401 |
Chain | Residue |
F | HIS151 |
F | ARG152 |
F | SER226 |
F | HIS298 |
F | ARG299 |
F | SER314 |
F | SER316 |
F | C2Z402 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue C2Z F 402 |
Chain | Residue |
F | ARG70 |
F | THR87 |
F | THR89 |
F | HIS151 |
F | SER226 |
F | SER242 |
F | LYS243 |
F | PHE244 |
F | HIS298 |
F | ARG299 |
F | C2Z401 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKiGehqltghk..........VAVK |
Chain | Residue | Details |
A | LEU22-LYS45 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL |
Chain | Residue | Details |
A | VAL135-LEU147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
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_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"UniProtKB","id":"Q5EG47","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
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_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
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_FI9 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80386","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
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_FI11 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R078","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 120 |
Details | Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 124 |
Details | Domain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 124 |
Details | Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 42 |
Details | Motif: {"description":"AMPK pseudosubstrate"} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 32 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 16 |
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_FI19 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |