1BH2
A326S MUTANT OF AN INHIBITORY ALPHA SUBUNIT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0007165 | biological_process | signal transduction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0007188 | biological_process | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
| A | 0019001 | molecular_function | guanyl nucleotide binding |
| A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 357 |
| Chain | Residue |
| A | SER47 |
| A | THR181 |
| A | GSP355 |
| A | HOH413 |
| A | HOH532 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE GSP A 355 |
| Chain | Residue |
| A | SER47 |
| A | THR48 |
| A | SER151 |
| A | LEU175 |
| A | ARG176 |
| A | THR177 |
| A | ARG178 |
| A | THR181 |
| A | GLY202 |
| A | GLY203 |
| A | GLN204 |
| A | ASN269 |
| A | LYS270 |
| A | ASP272 |
| A | LEU273 |
| A | CYS325 |
| A | SER326 |
| A | THR327 |
| A | MG357 |
| A | HOH401 |
| A | HOH402 |
| A | HOH403 |
| A | HOH413 |
| A | HOH532 |
| A | GLU43 |
| A | SER44 |
| A | GLY45 |
| A | LYS46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ |
| Chain | Residue | Details |
| A | SER44 | |
| A | ARG176 | |
| A | VAL201 | |
| A | LYS270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO |
| Chain | Residue | Details |
| A | THR48 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:4N0D |
| Chain | Residue | Details |
| A | SER151 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO |
| Chain | Residue | Details |
| A | THR182 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ |
| Chain | Residue | Details |
| A | THR327 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 8073283, 10507001, 8710841, 15236956, 9383480, 15128951 |
| Chain | Residue | Details |
| A | THR181 | |
| A | GLN204 | |
| A | GLU43 | |
| A | ARG178 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| A | SER44 | electrostatic stabiliser |
| A | ILE49 | electrostatic stabiliser |
| A | VAL179 | electrostatic stabiliser |
| A | VAL201 | electrostatic stabiliser |
| A | ARG205 | electrostatic stabiliser |
