6MS9
GDP-bound KRAS P34R mutant
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 |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0007165 | biological_process | signal transduction |
| C | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue GDP C 201 |
| Chain | Residue |
| C | GLY13 |
| C | LYS117 |
| C | ASP119 |
| C | LEU120 |
| C | SER145 |
| C | ALA146 |
| C | LYS147 |
| C | MG202 |
| C | HOH317 |
| C | HOH323 |
| C | HOH350 |
| C | VAL14 |
| C | HOH366 |
| C | HOH384 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| C | VAL29 |
| C | ASN116 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 202 |
| Chain | Residue |
| C | SER17 |
| C | ASP57 |
| C | GDP201 |
| C | HOH350 |
| C | HOH409 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue GDP B 201 |
| Chain | Residue |
| B | GLY13 |
| 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 | LYS147 |
| B | MG202 |
| B | HOH309 |
| B | HOH321 |
| B | HOH330 |
| B | HOH358 |
| B | HOH360 |
| B | HOH365 |
| B | HOH379 |
| B | HOH391 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | SER17 |
| B | GDP201 |
| B | HOH309 |
| B | HOH330 |
| B | HOH358 |
| B | HOH389 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue GDP A 201 |
| Chain | Residue |
| A | GLY13 |
| A | VAL14 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | LEU120 |
| A | SER145 |
| A | ALA146 |
| A | LYS147 |
| A | HOH308 |
| A | HOH310 |
| A | HOH320 |
| A | HOH328 |
| A | HOH392 |
| A | HOH393 |
| A | HOH397 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| 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_FI2 |
| Number of Residues | 3 |
| 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_FI3 |
| Number of Residues | 3 |
| 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_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
