5VPZ
Crystal structure of human KRAS G12A mutant in complex with GTP-gamma-S
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 | 4 |
| Details | binding site for residue MG A 201 |
| Chain | Residue |
| A | SER17 |
| A | GSP202 |
| A | HOH304 |
| A | HOH334 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue GSP A 202 |
| Chain | Residue |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| A | ASP30 |
| A | PRO34 |
| A | ALA59 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | LEU120 |
| A | SER145 |
| A | ALA146 |
| A | LYS147 |
| A | MG201 |
| A | HOH323 |
| A | HOH334 |
| A | GLY13 |
| A | VAL14 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | SER17 |
| B | GSP202 |
| B | HOH311 |
| B | HOH340 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue GSP B 202 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | GLY15 |
| B | LYS16 |
| B | SER17 |
| B | ALA18 |
| B | PHE28 |
| B | VAL29 |
| B | ASP30 |
| B | PRO34 |
| B | ALA59 |
| B | ASN116 |
| B | LYS117 |
| B | ASP119 |
| B | LEU120 |
| B | SER145 |
| B | ALA146 |
| B | LYS147 |
| B | MG201 |
| B | HOH311 |
| B | HOH340 |
| B | HOH352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| 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 | 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_FI3 |
| 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_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
