6UKA
Crystal structure of RHOG and ELMO complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005886 | cellular_component | plasma membrane |
A | 0005925 | cellular_component | focal adhesion |
A | 0007015 | biological_process | actin filament organization |
A | 0007163 | biological_process | establishment or maintenance of cell polarity |
A | 0007264 | biological_process | small GTPase-mediated signal transduction |
A | 0007266 | biological_process | Rho protein signal transduction |
A | 0008284 | biological_process | positive regulation of cell population proliferation |
A | 0008360 | biological_process | regulation of cell shape |
A | 0016020 | cellular_component | membrane |
A | 0016601 | biological_process | Rac protein signal transduction |
A | 0019901 | molecular_function | protein kinase binding |
A | 0030036 | biological_process | actin cytoskeleton organization |
A | 0030667 | cellular_component | secretory granule membrane |
A | 0030865 | biological_process | cortical cytoskeleton organization |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0032956 | biological_process | regulation of actin cytoskeleton organization |
A | 0042995 | cellular_component | cell projection |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0060326 | biological_process | cell chemotaxis |
A | 0070062 | cellular_component | extracellular exosome |
A | 0090630 | biological_process | activation of GTPase activity |
A | 0098794 | cellular_component | postsynapse |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0150052 | biological_process | regulation of postsynapse assembly |
A | 1900027 | biological_process | regulation of ruffle assembly |
A | 1903078 | biological_process | positive regulation of protein localization to plasma membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue GNP A 201 |
Chain | Residue |
A | GLY12 |
A | PRO34 |
A | THR35 |
A | GLY60 |
A | LYS116 |
A | ASP118 |
A | LEU119 |
A | SER158 |
A | ALA159 |
A | LEU160 |
A | MG202 |
A | ALA13 |
A | HOH314 |
A | HOH317 |
A | HOH321 |
A | HOH329 |
A | HOH349 |
A | HOH352 |
A | VAL14 |
A | GLY15 |
A | LYS16 |
A | THR17 |
A | CYS18 |
A | PHE28 |
A | TYR32 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | THR17 |
A | THR35 |
A | GNP201 |
A | HOH314 |
A | HOH317 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:18034455 |
Chain | Residue | Details |
B | TYR48 | |
A | THR115 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P62820 |
Chain | Residue | Details |
A | PHE28 | |
A | ASP57 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylasparagine; by botulinum toxin => ECO:0000250|UniProtKB:P61586 |
Chain | Residue | Details |
A | ASN39 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR138 | |
A | THR180 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P61586 |
Chain | Residue | Details |
A | CYS188 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | LIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P61586 |
Chain | Residue | Details |
A | CYS188 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: (Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate => ECO:0000269|PubMed:24905543 |
Chain | Residue | Details |
A | THR35 |