6P8X
Crystal structure of human KRAS G12C covalently bound to an acryloylazetidine acetamide inhibitor.
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 | 6 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | SER17 |
| A | GDP304 |
| A | HOH413 |
| A | HOH421 |
| A | HOH425 |
| A | HOH442 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | HOH423 |
| A | HOH452 |
| A | GLU63 |
| A | GLY138 |
| A | HOH422 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | ASP105 |
| A | HOH428 |
| A | HOH445 |
| C | HOH402 |
| C | HOH421 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue GDP A 304 |
| Chain | Residue |
| A | GLY13 |
| A | VAL14 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| A | ASP30 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | SER145 |
| A | ALA146 |
| A | LYS147 |
| A | CA301 |
| A | O5V305 |
| A | HOH404 |
| A | HOH413 |
| A | HOH440 |
| A | HOH442 |
| C | MET1 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue O5V A 305 |
| Chain | Residue |
| A | GLY10 |
| A | CYS12 |
| A | LYS16 |
| A | PRO34 |
| A | ALA59 |
| A | GLY60 |
| A | GLN61 |
| A | MET72 |
| A | ASP92 |
| A | HIS95 |
| A | TYR96 |
| A | GLN99 |
| A | ILE100 |
| A | GDP304 |
| A | HOH414 |
| A | HOH442 |
| D | HIS95 |
| D | O5V304 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 301 |
| Chain | Residue |
| B | SER17 |
| B | GDP304 |
| B | HOH410 |
| B | HOH412 |
| B | HOH413 |
| B | HOH429 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 302 |
| Chain | Residue |
| B | GLU63 |
| B | GLY138 |
| B | HOH417 |
| B | HOH421 |
| B | HOH440 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 303 |
| Chain | Residue |
| B | ASP105 |
| B | HOH411 |
| D | HOH401 |
| D | HOH406 |
| D | HOH445 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue GDP B 304 |
| 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 | CA301 |
| B | O5V305 |
| B | HOH412 |
| B | HOH429 |
| B | HOH433 |
| D | MET1 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 301 |
| Chain | Residue |
| C | HOH437 |
| C | SER17 |
| C | GDP303 |
| C | HOH408 |
| C | HOH413 |
| C | HOH417 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 302 |
| Chain | Residue |
| C | GLU63 |
| C | GLY138 |
| C | HOH404 |
| C | HOH407 |
| C | HOH427 |
| C | HOH432 |
| site_id | AD3 |
| Number of Residues | 20 |
| Details | binding site for residue GDP C 303 |
| Chain | Residue |
| C | GLY13 |
| C | VAL14 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| C | VAL29 |
| C | ASP30 |
| C | ASN116 |
| C | LYS117 |
| C | ASP119 |
| C | LEU120 |
| C | SER145 |
| C | ALA146 |
| C | LYS147 |
| C | CA301 |
| C | HOH413 |
| C | HOH420 |
| C | HOH437 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 301 |
| Chain | Residue |
| D | SER17 |
| D | GDP303 |
| D | HOH407 |
| D | HOH423 |
| D | HOH429 |
| D | HOH439 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 302 |
| Chain | Residue |
| D | GLU63 |
| D | GLY138 |
| D | HOH403 |
| D | HOH421 |
| D | HOH447 |
| D | HOH456 |
| site_id | AD6 |
| Number of Residues | 21 |
| Details | binding site for residue GDP D 303 |
| Chain | Residue |
| D | GLY13 |
| D | VAL14 |
| D | GLY15 |
| D | LYS16 |
| D | SER17 |
| D | ALA18 |
| D | PHE28 |
| D | VAL29 |
| D | ASP30 |
| D | ASN116 |
| D | LYS117 |
| D | ASP119 |
| D | LEU120 |
| D | SER145 |
| D | ALA146 |
| D | LYS147 |
| D | CA301 |
| D | O5V304 |
| D | HOH429 |
| D | HOH439 |
| D | HOH440 |
| site_id | AD7 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide O5V B 305 and CYS B 12 |
| Chain | Residue |
| B | GLY10 |
| B | ALA11 |
| B | GLY13 |
| B | VAL14 |
| B | LYS16 |
| B | PRO34 |
| B | ALA59 |
| B | GLY60 |
| B | GLN61 |
| B | GLU63 |
| B | MET72 |
| B | ASP92 |
| B | HIS95 |
| B | TYR96 |
| B | GLN99 |
| B | ILE100 |
| B | GDP304 |
| B | HOH415 |
| B | HOH425 |
| B | HOH429 |
| C | HIS95 |
| C | O5V304 |
| site_id | AD8 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide O5V C 304 and CYS C 12 |
| Chain | Residue |
| B | HIS95 |
| B | O5V305 |
| C | GLY10 |
| C | ALA11 |
| C | GLY13 |
| C | VAL14 |
| C | LYS16 |
| C | ALA59 |
| C | GLY60 |
| C | ARG68 |
| C | MET72 |
| C | ASP92 |
| C | HIS95 |
| C | TYR96 |
| C | GLN99 |
| C | ILE100 |
| C | HOH428 |
| site_id | AD9 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide O5V D 304 and CYS D 12 |
| Chain | Residue |
| A | HIS95 |
| A | O5V305 |
| D | GLY10 |
| D | ALA11 |
| D | GLY13 |
| D | VAL14 |
| D | LYS16 |
| D | ALA59 |
| D | GLY60 |
| D | GLN61 |
| D | ARG68 |
| D | MET72 |
| D | ASP92 |
| D | TYR96 |
| D | ILE100 |
| D | GDP303 |
| D | HOH430 |
| D | HOH439 |
| D | HOH446 |
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-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 | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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 |
| site_id | SWS_FT_FI6 |
| 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 |
