2GCN
Crystal structure of the human RhoC-GDP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000281 | biological_process | mitotic cytokinesis |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007165 | biological_process | signal transduction |
| A | 0007264 | biological_process | small GTPase-mediated signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0016477 | biological_process | cell migration |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0031334 | biological_process | positive regulation of protein-containing complex assembly |
| A | 0032154 | cellular_component | cleavage furrow |
| A | 0032420 | cellular_component | stereocilium |
| A | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| A | 0043297 | biological_process | apical junction assembly |
| A | 0044319 | biological_process | wound healing, spreading of cells |
| A | 0051496 | biological_process | positive regulation of stress fiber assembly |
| A | 0060193 | biological_process | positive regulation of lipase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1902766 | biological_process | skeletal muscle satellite cell migration |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 2001 |
| Chain | Residue |
| A | THR19 |
| A | THR37 |
| A | GDP1001 |
| A | HOH3143 |
| A | HOH3144 |
| A | HOH3145 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDP A 1001 |
| Chain | Residue |
| A | LYS18 |
| A | THR19 |
| A | CYS20 |
| A | PHE30 |
| A | VAL35 |
| A | LYS118 |
| A | ASP120 |
| A | LEU121 |
| A | SER160 |
| A | ALA161 |
| A | LYS162 |
| A | MG2001 |
| A | HOH3011 |
| A | HOH3046 |
| A | HOH3049 |
| A | HOH3059 |
| A | HOH3079 |
| A | HOH3143 |
| A | HOH3144 |
| A | HOH3145 |
| A | HOH3197 |
| A | ALA15 |
| A | CYS16 |
| A | GLY17 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 3001 |
| Chain | Residue |
| A | PHE154 |
| A | THR163 |
| A | GLU165 |
| A | HOH3073 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 3002 |
| Chain | Residue |
| A | ARG122 |
| A | ALA177 |
| A | GLY178 |
| A | LEU179 |
| A | EDO3003 |
| A | HOH3102 |
| A | HOH3117 |
| A | HOH3118 |
| A | HOH3125 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 3003 |
| Chain | Residue |
| A | ARG176 |
| A | LEU179 |
| A | EDO3002 |
| A | HOH3051 |
| A | HOH3179 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 3004 |
| Chain | Residue |
| A | GLY62 |
| A | ASP67 |
| A | ARG70 |
| A | LYS98 |
| A | TRP99 |
| A | HOH3044 |
| A | HOH3122 |
| A | HOH3163 |
| A | HOH3188 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 3005 |
| Chain | Residue |
| A | ILE43 |
| A | ASP45 |
| A | ASP90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB","evidences":[{"source":"PubMed","id":"24905543","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | GLN63 |
