2XNS
Crystal Structure Of Human G alpha i1 Bound To A Designed Helical Peptide Derived From The Goloco Motif Of RGS14
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 | 0005654 | cellular_component | nucleoplasm |
A | 0005730 | cellular_component | nucleolus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0005794 | cellular_component | Golgi apparatus |
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 | 0007189 | biological_process | adenylate cyclase-activating 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 | 0007218 | biological_process | neuropeptide 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 | 0034451 | cellular_component | centriolar satellite |
A | 0034695 | biological_process | response to prostaglandin E |
A | 0036064 | cellular_component | ciliary basal body |
A | 0043434 | biological_process | response to peptide hormone |
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 | 0051301 | biological_process | cell division |
A | 0060236 | biological_process | regulation of mitotic spindle organization |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070098 | biological_process | chemokine-mediated signaling pathway |
A | 0072678 | biological_process | T cell migration |
A | 1901082 | biological_process | positive regulation of relaxation of smooth muscle |
A | 1904322 | biological_process | cellular response to forskolin |
A | 1904778 | biological_process | positive regulation of protein localization to cell cortex |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001664 | molecular_function | G protein-coupled receptor binding |
B | 0003924 | molecular_function | GTPase activity |
B | 0003925 | molecular_function | G protein activity |
B | 0005515 | molecular_function | protein binding |
B | 0005525 | molecular_function | GTP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005730 | cellular_component | nucleolus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005765 | cellular_component | lysosomal membrane |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005813 | cellular_component | centrosome |
B | 0005829 | cellular_component | cytosol |
B | 0005834 | cellular_component | heterotrimeric G-protein complex |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005886 | cellular_component | plasma membrane |
B | 0005938 | cellular_component | cell cortex |
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 | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
B | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
B | 0007198 | biological_process | adenylate cyclase-inhibiting serotonin receptor signaling pathway |
B | 0007218 | biological_process | neuropeptide signaling pathway |
B | 0010854 | molecular_function | adenylate cyclase regulator activity |
B | 0010855 | molecular_function | adenylate cyclase inhibitor activity |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019001 | molecular_function | guanyl nucleotide binding |
B | 0019003 | molecular_function | GDP binding |
B | 0030496 | cellular_component | midbody |
B | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
B | 0031749 | molecular_function | D2 dopamine receptor binding |
B | 0031821 | molecular_function | G protein-coupled serotonin receptor binding |
B | 0034451 | cellular_component | centriolar satellite |
B | 0034695 | biological_process | response to prostaglandin E |
B | 0036064 | cellular_component | ciliary basal body |
B | 0043434 | biological_process | response to peptide hormone |
B | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
B | 0046676 | biological_process | negative regulation of insulin secretion |
B | 0046872 | molecular_function | metal ion binding |
B | 0051301 | biological_process | cell division |
B | 0060236 | biological_process | regulation of mitotic spindle organization |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070098 | biological_process | chemokine-mediated signaling pathway |
B | 0072678 | biological_process | T cell migration |
B | 1901082 | biological_process | positive regulation of relaxation of smooth muscle |
B | 1904322 | biological_process | cellular response to forskolin |
B | 1904778 | biological_process | positive regulation of protein localization to cell cortex |
C | 0030695 | molecular_function | GTPase regulator activity |
D | 0030695 | molecular_function | GTPase regulator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDP A 1348 |
Chain | Residue |
A | GLY42 |
A | ARG176 |
A | ARG178 |
A | ASN269 |
A | LYS270 |
A | ASP272 |
A | LEU273 |
A | CYS325 |
A | ALA326 |
A | THR327 |
C | ARG516 |
A | GLU43 |
A | SER44 |
A | GLY45 |
A | LYS46 |
A | SER47 |
A | THR48 |
A | ASP150 |
A | SER151 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDP B 1348 |
Chain | Residue |
B | GLY42 |
B | GLU43 |
B | SER44 |
B | GLY45 |
B | LYS46 |
B | SER47 |
B | THR48 |
B | ASP150 |
B | SER151 |
B | ARG176 |
B | ARG178 |
B | ASN269 |
B | LYS270 |
B | ASP272 |
B | LEU273 |
B | CYS325 |
B | ALA326 |
B | THR327 |
D | ARG516 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 1535 |
Chain | Residue |
A | GLN147 |
A | ARG242 |
C | SER510 |
C | GLY511 |
C | HIS513 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 1535 |
Chain | Residue |
B | GLN147 |
B | ARG242 |
D | SER510 |
D | GLY511 |
D | HIS513 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SRT B 1349 |
Chain | Residue |
A | GLU275 |
A | THR295 |
A | GLU297 |
B | LYS271 |
B | HIS322 |
B | PHE323 |
B | ASN331 |
B | PHE334 |
B | VAL335 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SRT A 1349 |
Chain | Residue |
A | LYS271 |
A | HIS322 |
A | PHE323 |
A | ASN331 |
A | PHE334 |
B | GLU275 |
B | THR295 |
B | TYR296 |
B | GLU297 |
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 | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18434541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22383884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | Modified residue: {"description":"ADP-ribosylarginine; by cholera toxin","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Deamidated glutamine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 46 |
Details | Domain: {"description":"GoLoco","evidences":[{"source":"PROSITE-ProRule","id":"PRU00097","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |