Functional Information from GO Data
| Chain | GOid | namespace | contents |
| G | 0043087 | biological_process | regulation of GTPase activity |
| R | 0003924 | molecular_function | GTPase activity |
| R | 0005525 | molecular_function | GTP binding |
| R | 0007165 | biological_process | signal transduction |
| R | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG R 168 |
| Chain | Residue |
| R | SER17 |
| R | THR35 |
| R | GDP167 |
| R | AF3169 |
| R | HOH201 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDP R 167 |
| Chain | Residue |
| R | GLY13 |
| R | VAL14 |
| R | GLY15 |
| R | LYS16 |
| R | SER17 |
| R | ALA18 |
| R | PHE28 |
| R | VAL29 |
| R | ASP30 |
| R | THR35 |
| R | ASN116 |
| R | LYS117 |
| R | ASP119 |
| R | SER145 |
| R | ALA146 |
| R | MG168 |
| R | AF3169 |
| R | HOH201 |
| G | HOH220 |
| G | THR785 |
| G | ARG789 |
| R | GLY12 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AF3 R 169 |
| Chain | Residue |
| G | ARG789 |
| R | GLY12 |
| R | LYS16 |
| R | THR35 |
| R | GLY60 |
| R | GLN61 |
| R | GDP167 |
| R | MG168 |
| R | HOH230 |
Functional Information from PROSITE/UniProt
| site_id | PS00509 |
| Number of Residues | 15 |
| Details | RAS_GTPASE_ACTIV_1 Ras GTPase-activating proteins domain signature. GfVFLRLICPAILNP |
| Chain | Residue | Details |
| G | GLY898-PRO912 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| G | SER831 | |
| R | VAL29 | |
| R | ALA59 | |
| R | ASN116 | |
| R | SER145 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| R | CYS118 | |
| Chain | Residue | Details |
| R | THR35 | |
