5GT7
Crystal Structure of Arg-bound CASTOR1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
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 | small molecule 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 |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0034198 | biological_process | cellular response to amino acid starvation |
B | 0034618 | molecular_function | arginine binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0061700 | cellular_component | GATOR2 complex |
B | 0140299 | molecular_function | small molecule sensor activity |
B | 0140311 | molecular_function | protein sequestering activity |
B | 1903577 | biological_process | cellular response to L-arginine |
B | 1904262 | biological_process | negative regulation of TORC1 signaling |
B | 1904263 | biological_process | positive regulation of TORC1 signaling |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
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 | small molecule 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 |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0034198 | biological_process | cellular response to amino acid starvation |
D | 0034618 | molecular_function | arginine binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0061700 | cellular_component | GATOR2 complex |
D | 0140299 | molecular_function | small molecule sensor activity |
D | 0140311 | molecular_function | protein sequestering activity |
D | 1903577 | biological_process | cellular response to L-arginine |
D | 1904262 | biological_process | negative regulation of TORC1 signaling |
D | 1904263 | biological_process | positive regulation of TORC1 signaling |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ARG A 401 |
Chain | Residue |
A | SER111 |
A | SER299 |
A | THR300 |
A | PHE301 |
A | PHE303 |
A | ASP304 |
A | HOH527 |
A | HOH555 |
A | HOH557 |
A | VAL112 |
A | LEU273 |
A | GLY274 |
A | GLU277 |
A | CYS278 |
A | GLY279 |
A | ILE280 |
A | VAL281 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MLI A 402 |
Chain | Residue |
A | THR199 |
A | THR200 |
A | ASP203 |
A | HOH574 |
B | LEU33 |
B | PRO195 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MLI A 403 |
Chain | Residue |
A | PHE32 |
A | PRO195 |
A | HOH506 |
B | THR199 |
B | THR200 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MLI A 404 |
Chain | Residue |
A | GLU73 |
A | ALA74 |
A | THR75 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue ARG B 401 |
Chain | Residue |
B | SER111 |
B | VAL112 |
B | LEU273 |
B | GLY274 |
B | GLU277 |
B | GLY279 |
B | ILE280 |
B | VAL281 |
B | SER299 |
B | THR300 |
B | PHE301 |
B | PHE303 |
B | ASP304 |
B | HOH517 |
B | HOH538 |
B | HOH550 |
site_id | AC6 |
Number of Residues | 17 |
Details | binding site for residue ARG C 401 |
Chain | Residue |
C | SER111 |
C | VAL112 |
C | LEU273 |
C | GLY274 |
C | GLU277 |
C | CYS278 |
C | GLY279 |
C | ILE280 |
C | VAL281 |
C | SER299 |
C | THR300 |
C | PHE301 |
C | PHE303 |
C | ASP304 |
C | HOH549 |
C | HOH556 |
C | HOH581 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue MLI C 402 |
Chain | Residue |
C | THR199 |
C | THR200 |
C | ASP203 |
C | HOH582 |
C | HOH609 |
D | PHE32 |
D | PRO195 |
D | HOH527 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residue ARG D 401 |
Chain | Residue |
D | SER111 |
D | VAL112 |
D | LEU113 |
D | LEU273 |
D | GLY274 |
D | GLU277 |
D | CYS278 |
D | GLY279 |
D | ILE280 |
D | VAL281 |
D | SER299 |
D | THR300 |
D | PHE301 |
D | PHE303 |
D | ASP304 |
D | HOH546 |
D | HOH568 |
D | HOH585 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue MLI D 402 |
Chain | Residue |
D | ARG11 |
D | ALA74 |
D | THR75 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MLI D 403 |
Chain | Residue |
C | PHE32 |
D | THR199 |
D | THR200 |
D | ASP203 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27487210, ECO:0007744|PDB:5I2C |
Chain | Residue | Details |
A | SER111 | |
C | GLY274 | |
C | ILE280 | |
C | THR300 | |
D | SER111 | |
D | GLY274 | |
D | ILE280 | |
D | THR300 | |
A | GLY274 | |
A | ILE280 | |
A | THR300 | |
B | SER111 | |
B | GLY274 | |
B | ILE280 | |
B | THR300 | |
C | SER111 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:33594058 |
Chain | Residue | Details |
A | SER14 | |
B | SER14 | |
C | SER14 | |
D | SER14 |