6M8H
Crystal Structure of the R208Q mutant of G(i) subunit alpha-1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0001664 | molecular_function | G protein-coupled receptor binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0003925 | molecular_function | G protein 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 | 0005829 | cellular_component | cytosol |
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 | 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 | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
A | 0007198 | biological_process | adenylate cyclase-inhibiting serotonin receptor signaling pathway |
A | 0010854 | molecular_function | adenylate cyclase regulator activity |
A | 0016787 | molecular_function | hydrolase activity |
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 | 0034695 | biological_process | response to prostaglandin E |
A | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
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 | 0072678 | biological_process | T cell migration |
A | 0098794 | cellular_component | postsynapse |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0099645 | biological_process | neurotransmitter receptor localization to postsynaptic specialization membrane |
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 | 30 |
Details | binding site for residue GSP A 401 |
Chain | Residue |
A | GLY42 |
A | ARG176 |
A | THR177 |
A | ARG178 |
A | THR181 |
A | GLY202 |
A | GLY203 |
A | ASN269 |
A | LYS270 |
A | ASP272 |
A | LEU273 |
A | GLU43 |
A | CYS325 |
A | ALA326 |
A | THR327 |
A | MG402 |
A | HOH514 |
A | HOH528 |
A | HOH536 |
A | HOH553 |
A | HOH566 |
A | HOH579 |
A | SER44 |
A | HOH617 |
A | GLY45 |
A | LYS46 |
A | SER47 |
A | THR48 |
A | SER151 |
A | LEU175 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | SER47 |
A | THR181 |
A | ASP200 |
A | GSP401 |
A | HOH514 |
A | HOH528 |
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 |