1ZW6
Crystal Structure of the GTP-bound form of RasQ61G
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 269 |
Chain | Residue |
A | SER17 |
A | THR35 |
A | GNP268 |
A | HOH272 |
A | HOH434 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 201 |
Chain | Residue |
A | HOH277 |
A | HOH304 |
A | PHE28 |
A | ASP30 |
A | GLU31 |
A | ASP33 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CA A 202 |
Chain | Residue |
A | ARG102 |
A | ARG102 |
A | ASP105 |
A | ASP105 |
A | HOH310 |
A | HOH310 |
A | HOH341 |
A | HOH341 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MG A 203 |
Chain | Residue |
A | GLY138 |
A | GLN165 |
A | HOH360 |
A | HOH366 |
A | HOH419 |
A | HOH431 |
A | HOH431 |
A | HOH435 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 204 |
Chain | Residue |
A | HOH279 |
A | HOH279 |
A | HOH279 |
A | HOH308 |
A | HOH308 |
A | HOH308 |
site_id | AC6 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE GNP A 268 |
Chain | Residue |
A | GLY12 |
A | GLY13 |
A | VAL14 |
A | GLY15 |
A | LYS16 |
A | SER17 |
A | ALA18 |
A | PHE28 |
A | VAL29 |
A | ASP30 |
A | GLU31 |
A | TYR32 |
A | PRO34 |
A | THR35 |
A | GLY60 |
A | ASN116 |
A | LYS117 |
A | ASP119 |
A | LEU120 |
A | SER145 |
A | ALA146 |
A | LYS147 |
A | MG269 |
A | HOH272 |
A | HOH276 |
A | HOH290 |
A | HOH309 |
A | HOH321 |
A | HOH353 |
A | HOH357 |
A | HOH434 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | GLY61 |