3V00
Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation.
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 |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0007165 | biological_process | signal transduction |
| C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| C | 0007188 | biological_process | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
| C | 0019001 | molecular_function | guanyl nucleotide binding |
| C | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP C 401 |
| Chain | Residue |
| C | GLY38 |
| C | ARG172 |
| C | ARG174 |
| C | ASN265 |
| C | LYS266 |
| C | ASP268 |
| C | LEU269 |
| C | CYS321 |
| C | ALA322 |
| C | THR323 |
| C | HOH515 |
| C | GLU39 |
| C | HOH519 |
| C | SER40 |
| C | GLY41 |
| C | LYS42 |
| C | SER43 |
| C | THR44 |
| C | SER147 |
| C | LEU171 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 401 |
| Chain | Residue |
| B | ALA37 |
| B | GLY38 |
| B | GLU39 |
| B | SER40 |
| B | GLY41 |
| B | LYS42 |
| B | SER43 |
| B | THR44 |
| B | SER147 |
| B | LEU171 |
| B | ARG172 |
| B | ARG174 |
| B | ASN265 |
| B | LYS266 |
| B | ASP268 |
| B | LEU269 |
| B | CYS321 |
| B | ALA322 |
| B | THR323 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GDP A 401 |
| Chain | Residue |
| A | GLU39 |
| A | SER40 |
| A | GLY41 |
| A | LYS42 |
| A | SER43 |
| A | THR44 |
| A | SER147 |
| A | LEU171 |
| A | ARG172 |
| A | SER173 |
| A | ARG174 |
| A | ASN265 |
| A | LYS266 |
| A | ASP268 |
| A | LEU269 |
| A | CYS321 |
| A | ALA322 |
| A | THR323 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7969474, ECO:0000269|PubMed:8208289, ECO:0000269|PubMed:8259210, ECO:0007744|PDB:1FQJ, ECO:0007744|PDB:1FQK, ECO:0007744|PDB:1GOT, ECO:0007744|PDB:1TAD, ECO:0007744|PDB:1TAG, ECO:0007744|PDB:1TND, ECO:0007744|PDB:3V00 |
| Chain | Residue | Details |
| C | GLY36 | |
| C | ASP146 | |
| C | LEU171 | |
| B | GLY36 | |
| B | ASP146 | |
| B | LEU171 | |
| A | GLY36 | |
| A | ASP146 | |
| A | LEU171 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01230 |
| Chain | Residue | Details |
| C | SER43 | |
| C | THR177 | |
| B | SER43 | |
| B | THR177 | |
| A | SER43 | |
| A | THR177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8259210, ECO:0007744|PDB:1TND |
| Chain | Residue | Details |
| C | GLY199 | |
| C | ALA322 | |
| B | GLY199 | |
| B | ALA322 | |
| A | GLY199 | |
| A | ALA322 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11488 |
| Chain | Residue | Details |
| C | TYR142 | |
| B | TYR142 | |
| A | TYR142 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820 |
| Chain | Residue | Details |
| C | GLY2 | |
| B | GLY2 | |
| A | GLY2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| 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 |
| C | ASN265 | |
| B | ASN265 | |
| A | ASN265 |
