3TDH
Structure of the regulatory fragment of sccharomyces cerevisiae AMPK in complex with AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005641 | cellular_component | nuclear envelope lumen |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006110 | biological_process | regulation of glycolytic process |
| C | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| C | 0006914 | biological_process | autophagy |
| C | 0007031 | biological_process | peroxisome organization |
| C | 0016208 | molecular_function | AMP binding |
| C | 0019887 | molecular_function | protein kinase regulator activity |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0030447 | biological_process | filamentous growth |
| C | 0031588 | cellular_component | nucleotide-activated protein kinase complex |
| C | 0042149 | biological_process | cellular response to glucose starvation |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| C | 0043609 | biological_process | regulation of carbon utilization |
| C | 0045722 | biological_process | positive regulation of gluconeogenesis |
| C | 1904547 | biological_process | regulation of cellular response to glucose starvation |
| C | 2000217 | biological_process | regulation of invasive growth in response to glucose limitation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AMP C 323 |
| Chain | Residue |
| C | THR195 |
| C | SER311 |
| C | ASP312 |
| C | HOH358 |
| C | HOH410 |
| C | ASN198 |
| C | LYS200 |
| C | VAL220 |
| C | SER221 |
| C | SER222 |
| C | PRO224 |
| C | VAL307 |
| C | THR309 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"24108357","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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_FI4 |
| Number of Residues | 63 |
| Details | Domain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 59 |
| Details | Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q10343","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22019086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T4N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
