6WS2
Crystal structure of KRAS-K104Q mutant, GDP-bound
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 |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0007165 | biological_process | signal transduction |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue GDP A 201 |
| Chain | Residue |
| A | GLY13 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | LEU120 |
| A | SER145 |
| A | ALA146 |
| A | LYS147 |
| A | MG202 |
| A | HOH311 |
| A | HOH331 |
| A | VAL14 |
| A | HOH335 |
| A | HOH343 |
| A | HOH351 |
| A | HOH360 |
| A | HOH390 |
| A | HOH392 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| A | ASP30 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | SER17 |
| A | GDP201 |
| A | HOH331 |
| A | HOH343 |
| A | HOH351 |
| A | HOH359 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | SER65 |
| A | ALA66 |
| A | MET67 |
| A | HOH325 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | ARG102 |
| A | HOH304 |
| A | HOH306 |
| A | HOH384 |
| D | VAL45 |
| D | ASP47 |
| D | GLY48 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 205 |
| Chain | Residue |
| A | TYR40 |
| A | ARG41 |
| A | HOH312 |
| D | SER136 |
| D | HOH336 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 206 |
| Chain | Residue |
| A | HIS95 |
| A | GLU98 |
| A | ARG102 |
| site_id | AC7 |
| Number of Residues | 26 |
| 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 | HOH306 |
| B | HOH314 |
| B | HOH316 |
| B | HOH326 |
| B | HOH328 |
| B | HOH352 |
| B | HOH383 |
| B | HOH392 |
| B | HOH393 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | SER17 |
| B | GDP201 |
| B | HOH304 |
| B | HOH314 |
| B | HOH316 |
| B | HOH352 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| B | SER65 |
| B | ALA66 |
| B | MET67 |
| B | HOH309 |
| C | GLU107 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 204 |
| Chain | Residue |
| B | GLN99 |
| B | ARG102 |
| B | HOH317 |
| B | HOH347 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 205 |
| Chain | Residue |
| B | HOH346 |
| site_id | AD3 |
| Number of Residues | 24 |
| Details | binding site for residue GDP C 201 |
| Chain | Residue |
| C | VAL29 |
| C | ASP30 |
| C | TYR32 |
| C | ASN116 |
| C | LYS117 |
| C | ASP119 |
| C | SER145 |
| C | ALA146 |
| C | LYS147 |
| C | MG202 |
| C | HOH312 |
| C | HOH328 |
| C | HOH338 |
| C | HOH348 |
| C | HOH396 |
| C | HOH406 |
| C | HOH411 |
| C | GLY13 |
| C | VAL14 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 202 |
| Chain | Residue |
| C | SER17 |
| C | GDP201 |
| C | HOH312 |
| C | HOH320 |
| C | HOH343 |
| C | HOH348 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 203 |
| Chain | Residue |
| C | ARG97 |
| C | LYS101 |
| C | HOH380 |
| site_id | AD6 |
| Number of Residues | 23 |
| Details | binding site for residue GDP D 201 |
| Chain | Residue |
| D | GLY13 |
| D | VAL14 |
| D | GLY15 |
| D | LYS16 |
| D | SER17 |
| D | ALA18 |
| D | PHE28 |
| D | ASP30 |
| D | ASN116 |
| D | LYS117 |
| D | ASP119 |
| D | LEU120 |
| D | SER145 |
| D | ALA146 |
| D | LYS147 |
| D | MG202 |
| D | HOH316 |
| D | HOH333 |
| D | HOH337 |
| D | HOH354 |
| D | HOH364 |
| D | HOH378 |
| D | HOH379 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 202 |
| Chain | Residue |
| D | SER17 |
| D | GDP201 |
| D | HOH311 |
| D | HOH333 |
| D | HOH337 |
| D | HOH346 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Effector region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 72 |
| 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 | 4 |
| 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 | 4 |
| 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 | 4 |
| 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 | 4 |
| 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 |
