4PAM
A conserved phenylalanine as relay between the 5 helix and the GDP binding region of heterotrimeric G protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001664 | molecular_function | G protein-coupled receptor binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005834 | cellular_component | heterotrimeric G-protein complex |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005938 | cellular_component | cell cortex |
| A | 0007049 | biological_process | cell cycle |
| 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 | 0016020 | cellular_component | membrane |
| A | 0019001 | molecular_function | guanyl nucleotide binding |
| A | 0019003 | molecular_function | GDP binding |
| A | 0030496 | cellular_component | midbody |
| A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| A | 0031749 | molecular_function | D2 dopamine receptor binding |
| A | 0031821 | molecular_function | G protein-coupled serotonin receptor binding |
| A | 0032794 | molecular_function | GTPase activating protein binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0043949 | biological_process | regulation of cAMP-mediated signaling |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050805 | biological_process | negative regulation of synaptic transmission |
| A | 0051301 | biological_process | cell division |
| A | 0060236 | biological_process | regulation of mitotic spindle organization |
| A | 1904322 | biological_process | cellular response to forskolin |
| A | 1904778 | biological_process | positive regulation of protein localization to cell cortex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue GDP A 401 |
| Chain | Residue |
| A | GLU43 |
| A | THR177 |
| A | ARG178 |
| A | ASN269 |
| A | LYS270 |
| A | ASP272 |
| A | LEU273 |
| A | CYS325 |
| A | ALA326 |
| A | THR327 |
| A | CL403 |
| A | SER44 |
| A | HOH537 |
| A | HOH541 |
| A | HOH542 |
| A | HOH543 |
| A | HOH549 |
| A | HOH551 |
| A | HOH582 |
| A | GLY45 |
| A | LYS46 |
| A | SER47 |
| A | THR48 |
| A | SER151 |
| A | LEU175 |
| A | ARG176 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO3 A 402 |
| Chain | Residue |
| A | ARG15 |
| A | ARG21 |
| A | ARG32 |
| A | LYS180 |
| A | HOH520 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ASP150 |
| A | ARG178 |
| A | LYS270 |
| A | GDP401 |
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 | GLU43 | |
| A | LEU175 | |
| A | ASP200 | |
| A | ASN269 |
| 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 | SER47 |
| 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 | ASP150 |
| 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 | THR181 |
| 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 | ALA326 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820 |
| Chain | Residue | Details |
| A | GLY2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26253820 |
| Chain | Residue | Details |
| A | CYS3 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| A | GLU43 | electrostatic stabiliser |
| A | THR48 | electrostatic stabiliser |
| A | ARG178 | electrostatic stabiliser |
| A | ASP200 | electrostatic stabiliser |
| A | GLN204 | electrostatic stabiliser |
