1SHZ
Crystal Structure of the p115RhoGEF rgRGS Domain in A Complex with Galpha(13):Galpha(i1) Chimera
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 |
| C | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 |
| F | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| F | 0005737 | cellular_component | cytoplasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 377 |
| Chain | Residue |
| A | SER62 |
| A | THR203 |
| A | ALF378 |
| A | GDP475 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 377 |
| Chain | Residue |
| D | SER62 |
| D | THR203 |
| D | ALF378 |
| D | GDP476 |
| D | HOH502 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF A 378 |
| Chain | Residue |
| A | GLY57 |
| A | GLU58 |
| A | LYS61 |
| A | ARG200 |
| A | THR203 |
| A | VAL223 |
| A | GLY225 |
| A | GLN226 |
| A | MG377 |
| A | GDP475 |
| A | HOH543 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ALF D 378 |
| Chain | Residue |
| D | GLY57 |
| D | GLU58 |
| D | LYS61 |
| D | ARG200 |
| D | PRO202 |
| D | THR203 |
| D | GLY225 |
| D | GLN226 |
| D | MG377 |
| D | GDP476 |
| D | HOH502 |
| D | HOH550 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDP A 475 |
| Chain | Residue |
| A | GLU58 |
| A | SER59 |
| A | GLY60 |
| A | LYS61 |
| A | SER62 |
| A | THR63 |
| A | LEU197 |
| A | LEU198 |
| A | ARG200 |
| A | ASN291 |
| A | LYS292 |
| A | ASP294 |
| A | LEU295 |
| A | ALA348 |
| A | THR349 |
| A | MG377 |
| A | ALF378 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GDP D 476 |
| Chain | Residue |
| D | GLU58 |
| D | SER59 |
| D | GLY60 |
| D | LYS61 |
| D | SER62 |
| D | THR63 |
| D | SER173 |
| D | LEU197 |
| D | LEU198 |
| D | ARG200 |
| D | ASN291 |
| D | LYS292 |
| D | ASP294 |
| D | CYS347 |
| D | ALA348 |
| D | THR349 |
| D | MG377 |
| D | ALF378 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | SER59 | |
| A | ASP222 | |
| A | ASN291 | |
| D | SER59 | |
| D | ASP222 | |
| D | ASN291 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO |
| Chain | Residue | Details |
| A | THR63 | |
| D | THR63 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1AS0, 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 | ALA348 | |
| D | ALA348 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX7 |
| Chain | Residue | Details |
| A | SER173 | |
| D | SER173 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB, ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7 |
| Chain | Residue | Details |
| A | LEU197 | |
| D | LEU197 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX6 |
| Chain | Residue | Details |
| A | THR203 | |
| D | THR203 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14344 |
| Chain | Residue | Details |
| A | THR203 | |
| D | THR203 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| A | SER59 | electrostatic stabiliser |
| A | ASP222 | electrostatic stabiliser |
| A | GLN226 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| D | SER59 | electrostatic stabiliser |
| D | ASP222 | electrostatic stabiliser |
| D | GLN226 | electrostatic stabiliser |
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | GLU58 | |
| A | GLN226 | |
| A | ARG200 | |
| A | THR203 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| D | GLU58 | |
| D | GLN226 | |
| D | ARG200 | |
| D | THR203 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | GLN226 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| D | GLN226 |
