6FA1
Antibody derived (Abd-4) small molecule binding to 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 |
| 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 |
| E | 0003924 | molecular_function | GTPase activity |
| E | 0005525 | molecular_function | GTP binding |
| E | 0007165 | biological_process | signal transduction |
| E | 0016020 | cellular_component | membrane |
| F | 0003924 | molecular_function | GTPase activity |
| F | 0005525 | molecular_function | GTP binding |
| F | 0007165 | biological_process | signal transduction |
| F | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | SER17 |
| B | THR35 |
| B | GNP202 |
| B | HOH317 |
| B | HOH337 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue GNP B 202 |
| Chain | Residue |
| B | LYS16 |
| B | SER17 |
| B | ALA18 |
| B | PHE28 |
| B | VAL29 |
| B | ASP30 |
| B | GLU31 |
| B | TYR32 |
| B | PRO34 |
| B | THR35 |
| B | GLY60 |
| B | ASN116 |
| B | LYS117 |
| B | ASP119 |
| B | LEU120 |
| B | SER145 |
| B | ALA146 |
| B | MG201 |
| B | HOH303 |
| B | HOH317 |
| B | HOH320 |
| B | HOH337 |
| B | HOH340 |
| B | HOH365 |
| B | GLY12 |
| B | GLY13 |
| B | VAL14 |
| B | GLY15 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue D2Z B 203 |
| Chain | Residue |
| B | LYS5 |
| B | LEU6 |
| B | ASP54 |
| B | GLN70 |
| B | TYR71 |
| B | THR74 |
| F | ASP105 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 201 |
| Chain | Residue |
| A | SER17 |
| A | THR35 |
| A | GNP202 |
| A | HOH309 |
| A | HOH327 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | binding site for residue GNP A 202 |
| 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 | MG201 |
| A | HOH301 |
| A | HOH306 |
| A | HOH309 |
| A | HOH324 |
| A | HOH327 |
| A | HOH371 |
| A | HOH372 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue D2Z A 203 |
| Chain | Residue |
| A | HIS61 |
| A | HIS95 |
| A | TYR96 |
| A | ILE139 |
| A | PRO140 |
| A | GLU162 |
| A | LYS165 |
| B | GLU31 |
| B | ASP33 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 201 |
| Chain | Residue |
| C | SER17 |
| C | THR35 |
| C | GNP202 |
| C | HOH316 |
| C | HOH318 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | binding site for residue GNP C 202 |
| Chain | Residue |
| C | TYR32 |
| C | PRO34 |
| C | THR35 |
| C | GLY60 |
| C | ASN116 |
| C | LYS117 |
| C | ASP119 |
| C | LEU120 |
| C | SER145 |
| C | ALA146 |
| C | MG201 |
| C | HOH316 |
| C | HOH318 |
| C | HOH323 |
| C | HOH333 |
| C | HOH350 |
| C | GLY12 |
| C | GLY13 |
| C | VAL14 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| C | VAL29 |
| C | ASP30 |
| C | GLU31 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | binding site for residue GNP D 201 |
| Chain | Residue |
| D | GLY12 |
| D | GLY13 |
| D | VAL14 |
| D | GLY15 |
| D | LYS16 |
| D | SER17 |
| D | ALA18 |
| D | PHE28 |
| D | VAL29 |
| D | ASP30 |
| D | GLU31 |
| D | TYR32 |
| D | PRO34 |
| D | THR35 |
| D | GLY60 |
| D | ASN116 |
| D | LYS117 |
| D | ASP119 |
| D | LEU120 |
| D | SER145 |
| D | ALA146 |
| D | MG202 |
| D | HOH301 |
| D | HOH306 |
| D | HOH308 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 202 |
| Chain | Residue |
| D | SER17 |
| D | THR35 |
| D | GNP201 |
| D | HOH306 |
| D | HOH308 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG E 201 |
| Chain | Residue |
| E | SER17 |
| E | THR35 |
| E | GNP202 |
| E | HOH306 |
| E | HOH318 |
| site_id | AD3 |
| Number of Residues | 25 |
| Details | binding site for residue GNP E 202 |
| Chain | Residue |
| E | GLY12 |
| E | GLY13 |
| E | VAL14 |
| E | GLY15 |
| E | LYS16 |
| E | SER17 |
| E | ALA18 |
| E | PHE28 |
| E | VAL29 |
| E | ASP30 |
| E | GLU31 |
| E | TYR32 |
| E | PRO34 |
| E | THR35 |
| E | GLY60 |
| E | ASN116 |
| E | LYS117 |
| E | ASP119 |
| E | SER145 |
| E | ALA146 |
| E | MG201 |
| E | HOH306 |
| E | HOH318 |
| E | HOH327 |
| E | HOH336 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG F 201 |
| Chain | Residue |
| F | SER17 |
| F | THR35 |
| F | GNP202 |
| F | HOH305 |
| F | HOH333 |
| site_id | AD5 |
| Number of Residues | 23 |
| Details | binding site for residue GNP F 202 |
| Chain | Residue |
| F | GLY12 |
| F | GLY13 |
| F | VAL14 |
| F | GLY15 |
| F | LYS16 |
| F | SER17 |
| F | ALA18 |
| F | PHE28 |
| F | VAL29 |
| F | ASP30 |
| F | TYR32 |
| F | PRO34 |
| F | THR35 |
| F | GLY60 |
| F | ASN116 |
| F | LYS117 |
| F | ASP119 |
| F | SER145 |
| F | ALA146 |
| F | MG201 |
| F | HOH305 |
| F | HOH333 |
| F | HOH361 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue D2Z F 203 |
| Chain | Residue |
| F | ASP54 |
| F | GLN70 |
| F | TYR71 |
| F | THR74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Motif: {"description":"Effector region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| 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 | 6 |
| 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 | 6 |
| 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 | 6 |
| 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 | 6 |
| 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 |
