4N0E
Crystal structure of the K345L variant of the Gi alpha1 subunit bound to GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001664 | molecular_function | G protein-coupled receptor binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0003925 | molecular_function | G protein activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005834 | cellular_component | heterotrimeric G-protein complex |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005938 | cellular_component | cell cortex |
| 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 | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
| A | 0007198 | biological_process | adenylate cyclase-inhibiting serotonin receptor signaling pathway |
| A | 0010854 | molecular_function | adenylate cyclase regulator activity |
| A | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019001 | molecular_function | guanyl nucleotide binding |
| A | 0019003 | molecular_function | GDP binding |
| A | 0030496 | cellular_component | midbody |
| A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| A | 0031749 | molecular_function | D2 dopamine receptor binding |
| A | 0031821 | molecular_function | G protein-coupled serotonin receptor binding |
| A | 0032794 | molecular_function | GTPase activating protein binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034695 | biological_process | response to prostaglandin E |
| A | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
| A | 0046676 | biological_process | negative regulation of insulin secretion |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050805 | biological_process | negative regulation of synaptic transmission |
| A | 0051301 | biological_process | cell division |
| A | 0060236 | biological_process | regulation of mitotic spindle organization |
| A | 0072678 | biological_process | T cell migration |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0099645 | biological_process | neurotransmitter receptor localization to postsynaptic specialization membrane |
| A | 1904322 | biological_process | cellular response to forskolin |
| A | 1904778 | biological_process | positive regulation of protein localization to cell cortex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDP A 401 |
| Chain | Residue |
| A | GLU43 |
| A | THR177 |
| A | ARG178 |
| A | ASN269 |
| A | LYS270 |
| A | ASP272 |
| A | LEU273 |
| A | CYS325 |
| A | ALA326 |
| A | THR327 |
| A | HOH515 |
| A | SER44 |
| A | HOH516 |
| A | HOH534 |
| A | HOH617 |
| A | HOH618 |
| A | HOH619 |
| A | GLY45 |
| A | LYS46 |
| A | SER47 |
| A | THR48 |
| A | SER151 |
| A | LEU175 |
| A | ARG176 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ARG15 |
| A | ARG21 |
| A | ARG32 |
| A | LYS180 |
| A | LEU348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 13 |
| 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 | 8 |
| 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 | 7 |
| Details | Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 11 |
| 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_FI6 |
| Number of Residues | 1 |
| 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_FI7 |
| Number of Residues | 1 |
| 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_FI8 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 533 |
| Chain | Residue | Details |
| A | GLU43 | electrostatic stabiliser |
| A | THR48 | electrostatic stabiliser |
| A | ARG178 | electrostatic stabiliser |
| A | ASP200 | electrostatic stabiliser |
