6VU8
Structure of G-alpha-i bound to its chaperone Ric-8A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001701 | biological_process | in utero embryonic development |
A | 0001944 | biological_process | vasculature development |
A | 0001965 | molecular_function | G-protein alpha-subunit binding |
A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006457 | biological_process | protein folding |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
A | 0007369 | biological_process | gastrulation |
A | 0008542 | biological_process | visual learning |
A | 0009416 | biological_process | response to light stimulus |
A | 0016020 | cellular_component | membrane |
A | 0042074 | biological_process | cell migration involved in gastrulation |
A | 0044183 | molecular_function | protein folding chaperone |
A | 0070586 | biological_process | cell-cell adhesion involved in gastrulation |
A | 0071711 | biological_process | basement membrane organization |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0007165 | biological_process | signal transduction |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0007188 | biological_process | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
B | 0019001 | molecular_function | guanyl nucleotide binding |
B | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21115486, ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q |
Chain | Residue | Details |
B | GLU43 | |
B | ASN269 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0 |
Chain | Residue | Details |
B | SER47 | |
B | THR59 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:4G5Q |
Chain | Residue | Details |
B | SER57 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q |
Chain | Residue | Details |
B | LEU58 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21115486 |
Chain | Residue | Details |
B | ASP200 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q |
Chain | Residue | Details |
B | ALA326 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250 |
Chain | Residue | Details |
B | ARG58 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704 |
Chain | Residue | Details |
B | GLN204 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250 |
Chain | Residue | Details |
B | CYS351 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805 |
Chain | Residue | Details |
B | GLY2 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824 |
Chain | Residue | Details |
B | CYS3 |