1WQ1
RAS-RASGAP COMPLEX
Functional Information from GO Data
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 (rasGAP) domain signature. GfVFLRLICPAILNP |
| Chain | Residue | Details |
| G | GLY898-PRO912 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Effector region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16698776","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine; in GTPase HRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylthreonine; in GTPase HRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"9020151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626575","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9632667","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 210 |
| Details | Domain: {"description":"Ras-GAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00167","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00167","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| 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 |
| R | GLN61 |
