5GV2
Crystal structure of Arginine-bound CASTOR1 from Homo sapiens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0034198 | biological_process | cellular response to amino acid starvation |
| A | 0034618 | molecular_function | arginine binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0061700 | cellular_component | GATOR2 complex |
| A | 0140299 | molecular_function | molecular sensor activity |
| A | 0140311 | molecular_function | protein sequestering activity |
| A | 1903577 | biological_process | cellular response to L-arginine |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
| A | 1904263 | biological_process | positive regulation of TORC1 signaling |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0034198 | biological_process | cellular response to amino acid starvation |
| C | 0034618 | molecular_function | arginine binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0061700 | cellular_component | GATOR2 complex |
| C | 0140299 | molecular_function | molecular sensor activity |
| C | 0140311 | molecular_function | protein sequestering activity |
| C | 1903577 | biological_process | cellular response to L-arginine |
| C | 1904262 | biological_process | negative regulation of TORC1 signaling |
| C | 1904263 | biological_process | positive regulation of TORC1 signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 501 |
| Chain | Residue |
| A | HIS108 |
| A | HIS135 |
| C | HIS108 |
| C | HIS135 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue ARG A 401 |
| Chain | Residue |
| A | CYS278 |
| A | GLY279 |
| A | ILE280 |
| A | VAL281 |
| A | SER299 |
| A | THR300 |
| A | PHE301 |
| A | PHE303 |
| A | ASP304 |
| A | HOH538 |
| A | HOH547 |
| A | SER111 |
| A | VAL112 |
| A | LEU273 |
| A | GLY274 |
| A | GLU277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Domain: {"description":"ACT 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 122 |
| Details | Domain: {"description":"ACT 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27487210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5I2C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"33594058","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
