4TQA
Crystal Structure of a GDP-bound G13D Oncogenic Mutant of Human GTPase KRas
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0007165 | biological_process | signal transduction |
A | 0016020 | cellular_component | membrane |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0007165 | biological_process | signal transduction |
B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | binding site for residue GDP A 201 |
Chain | Residue |
A | GLY0 |
A | ASP30 |
A | ASN116 |
A | LYS117 |
A | ASP119 |
A | LEU120 |
A | SER145 |
A | ALA146 |
A | LYS147 |
A | MG202 |
A | HOH303 |
A | ASP13 |
A | HOH316 |
A | HOH331 |
A | HOH341 |
A | HOH350 |
A | HOH376 |
A | HOH404 |
A | HOH407 |
A | VAL14 |
A | GLY15 |
A | LYS16 |
A | SER17 |
A | ALA18 |
A | PHE28 |
A | VAL29 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | SER17 |
A | GDP201 |
A | HOH316 |
A | HOH404 |
A | HOH406 |
A | HOH407 |
site_id | AC3 |
Number of Residues | 27 |
Details | binding site for residue GDP B 201 |
Chain | Residue |
B | GLY0 |
B | ASP13 |
B | VAL14 |
B | GLY15 |
B | LYS16 |
B | SER17 |
B | ALA18 |
B | PHE28 |
B | VAL29 |
B | ASP30 |
B | ASN116 |
B | LYS117 |
B | ASP119 |
B | LEU120 |
B | SER145 |
B | ALA146 |
B | MG202 |
B | HOH303 |
B | HOH315 |
B | HOH335 |
B | HOH337 |
B | HOH341 |
B | HOH347 |
B | HOH393 |
B | HOH423 |
B | HOH473 |
B | HOH521 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 202 |
Chain | Residue |
B | SER17 |
B | GDP201 |
B | HOH315 |
B | HOH422 |
B | HOH423 |
B | HOH521 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | Motif: {"description":"Effector region"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N-acetylmethionine; in GTPase KRas; 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 | 2 |
Details | Modified residue: {"description":"N-acetylthreonine; in GTPase KRas, 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 | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |