2G83
Structure of activated G-alpha-i1 bound to a nucleotide-state-selective peptide: Minimal determinants for recognizing the active form of a G protein 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 |
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 PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ALF A 357 |
Chain | Residue |
A | GLY42 |
A | MG356 |
A | GLU43 |
A | LYS46 |
A | ARG178 |
A | LYS180 |
A | THR181 |
A | GLY203 |
A | GLN204 |
A | GDP355 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ALF B 359 |
Chain | Residue |
B | HOH1 |
B | GLY42 |
B | GLU43 |
B | LYS46 |
B | ARG178 |
B | LYS180 |
B | THR181 |
B | VAL201 |
B | GLY202 |
B | GLY203 |
B | GLN204 |
B | GDP355 |
B | MG358 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 356 |
Chain | Residue |
A | SER47 |
A | ARG178 |
A | VAL179 |
A | THR181 |
A | GDP355 |
A | ALF357 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 358 |
Chain | Residue |
B | SER47 |
B | VAL179 |
B | THR181 |
B | GDP355 |
B | ALF359 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GDP A 355 |
Chain | Residue |
A | HOH2 |
A | HOH13 |
A | GLU43 |
A | SER44 |
A | GLY45 |
A | LYS46 |
A | SER47 |
A | THR48 |
A | SER151 |
A | LEU175 |
A | ARG176 |
A | THR177 |
A | ARG178 |
A | THR181 |
A | ASN269 |
A | LYS270 |
A | ASP272 |
A | LEU273 |
A | CYS325 |
A | ALA326 |
A | MG356 |
A | ALF357 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GDP B 355 |
Chain | Residue |
B | HOH1 |
B | GLU43 |
B | SER44 |
B | GLY45 |
B | LYS46 |
B | SER47 |
B | THR48 |
B | SER151 |
B | LEU175 |
B | ARG176 |
B | ARG178 |
B | THR181 |
B | ASN269 |
B | LYS270 |
B | ASP272 |
B | LEU273 |
B | CYS325 |
B | ALA326 |
B | MG358 |
B | ALF359 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
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 |
A | SER44 | |
A | LYS270 | |
B | SER44 | |
B | LYS270 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0 |
Chain | Residue | Details |
A | THR48 | |
A | THR182 | |
B | THR48 | |
B | THR182 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
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 |
A | ALA152 | |
B | ALA152 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
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 |
A | ARG176 | |
B | ARG176 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21115486 |
Chain | Residue | Details |
A | VAL201 | |
B | VAL201 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
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 |
A | THR327 | |
B | THR327 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250 |
Chain | Residue | Details |
A | VAL179 | |
B | VAL179 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704 |
Chain | Residue | Details |
A | ARG205 | |
B | ARG205 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | THR181 | |
A | GLN204 | |
A | GLU43 | |
A | ARG178 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | THR181 | |
B | GLN204 | |
B | GLU43 | |
B | ARG178 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | GLN204 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | GLN204 |