1FQJ
CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(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 | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| C | 0007601 | biological_process | visual perception |
| C | 0030553 | molecular_function | cGMP binding |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0007165 | biological_process | signal transduction |
| D | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| D | 0007188 | biological_process | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
| D | 0019001 | molecular_function | guanyl nucleotide binding |
| D | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| E | 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 | ARG174 |
| A | VAL175 |
| A | LYS176 |
| A | THR177 |
| A | VAL197 |
| A | GLY199 |
| A | GLN200 |
| A | MG352 |
| A | GDP360 |
| A | HOH363 |
| A | HOH364 |
| A | HOH365 |
| A | GLY38 |
| A | GLU39 |
| A | LYS42 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 352 |
| Chain | Residue |
| D | SER43 |
| D | THR177 |
| D | GDP361 |
| D | ALF363 |
| D | HOH365 |
| D | HOH366 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ALF D 363 |
| Chain | Residue |
| D | GLY38 |
| D | GLU39 |
| D | LYS42 |
| D | ARG174 |
| D | VAL175 |
| D | LYS176 |
| D | THR177 |
| D | VAL197 |
| D | GLY199 |
| D | GLN200 |
| D | MG352 |
| D | GDP361 |
| D | HOH364 |
| D | HOH365 |
| D | HOH366 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDP A 360 |
| Chain | Residue |
| 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 | HOH366 |
| A | HOH368 |
| A | HOH374 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDP D 361 |
| Chain | Residue |
| D | GLY38 |
| D | GLU39 |
| D | SER40 |
| D | GLY41 |
| D | LYS42 |
| D | SER43 |
| D | THR44 |
| D | ASP146 |
| D | SER147 |
| D | LEU171 |
| D | ARG172 |
| D | SER173 |
| D | ARG174 |
| D | ASN265 |
| D | LYS266 |
| D | ASP268 |
| D | LEU269 |
| D | CYS321 |
| D | ALA322 |
| D | THR323 |
| D | MG352 |
| D | ALF363 |
| D | HOH365 |
| D | HOH368 |
| D | HOH369 |
| D | HOH373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7969474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8208289","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8259210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FQJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FQK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GOT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V00","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19703466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8259210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TND","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11488","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 230 |
| Details | Domain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 |
| D | THR177 | |
| D | GLN200 | |
| D | GLU39 | |
| D | 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 |
| D | GLN200 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| A | GLU39 | electrostatic stabiliser |
| A | THR44 | electrostatic stabiliser |
| A | ARG174 | electrostatic stabiliser |
| A | ASP196 | electrostatic stabiliser |
| A | GLN200 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| D | GLU39 | electrostatic stabiliser |
| D | THR44 | electrostatic stabiliser |
| D | ARG174 | electrostatic stabiliser |
| D | ASP196 | electrostatic stabiliser |
| D | GLN200 | electrostatic stabiliser |






