1FQK
CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]
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 | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
| 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 |
| D | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 352 |
| Chain | Residue |
| A | SER43 |
| A | THR177 |
| A | GDP360 |
| A | ALF362 |
| A | HOH364 |
| A | HOH365 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ALF A 362 |
| Chain | Residue |
| A | LYS42 |
| A | ARG174 |
| A | VAL175 |
| A | LYS176 |
| A | THR177 |
| A | GLY199 |
| A | GLN200 |
| A | MG352 |
| A | GDP360 |
| A | HOH363 |
| A | HOH364 |
| A | HOH365 |
| A | ALA37 |
| A | GLY38 |
| A | GLU39 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 352 |
| Chain | Residue |
| C | SER43 |
| C | THR177 |
| C | GDP361 |
| C | ALF363 |
| C | HOH365 |
| C | HOH366 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ALF C 363 |
| Chain | Residue |
| C | GLY38 |
| C | GLU39 |
| C | LYS42 |
| C | ARG174 |
| C | VAL175 |
| C | LYS176 |
| C | THR177 |
| C | GLY199 |
| C | GLN200 |
| C | MG352 |
| C | GDP361 |
| C | HOH364 |
| C | HOH365 |
| C | HOH366 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDP A 360 |
| Chain | Residue |
| A | GLY38 |
| A | GLU39 |
| A | SER40 |
| A | GLY41 |
| A | LYS42 |
| A | SER43 |
| A | THR44 |
| A | ASP146 |
| A | SER147 |
| A | LEU171 |
| A | ARG172 |
| A | SER173 |
| A | ARG174 |
| A | ASN265 |
| A | LYS266 |
| A | ASP268 |
| A | LEU269 |
| A | CYS321 |
| A | ALA322 |
| A | THR323 |
| A | MG352 |
| A | ALF362 |
| A | HOH364 |
| A | HOH368 |
| A | HOH382 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDP C 361 |
| Chain | Residue |
| C | GLY38 |
| C | GLU39 |
| C | SER40 |
| C | GLY41 |
| C | LYS42 |
| C | SER43 |
| C | THR44 |
| C | ASP146 |
| C | SER147 |
| C | LEU171 |
| C | ARG172 |
| C | SER173 |
| C | ARG174 |
| C | ASN265 |
| C | LYS266 |
| C | ASP268 |
| C | CYS321 |
| C | ALA322 |
| C | THR323 |
| C | MG352 |
| C | ALF363 |
| C | HOH365 |
| C | HOH370 |
| C | HOH387 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 |
| A | GLY36 | |
| A | ASP146 | |
| A | LEU171 | |
| C | GLY36 | |
| C | ASP146 | |
| C | LEU171 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01230 |
| Chain | Residue | Details |
| A | SER43 | |
| A | THR177 | |
| C | SER43 | |
| C | THR177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8259210, ECO:0007744|PDB:1TND |
| Chain | Residue | Details |
| A | GLY199 | |
| A | ALA322 | |
| C | GLY199 | |
| C | ALA322 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11488 |
| Chain | Residue | Details |
| A | TYR142 | |
| C | TYR142 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 | ASN265 | |
| C | ASN265 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | THR177 | |
| A | GLN200 | |
| A | GLU39 | |
| A | ARG174 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| C | THR177 | |
| C | GLN200 | |
| C | GLU39 | |
| C | ARG174 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | GLN200 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| C | GLN200 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 533 |
| Chain | Residue | Details |
