6P0Z
Crystal structure of N-acetylated KRAS (2-169) bound to GDP and Mg
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 | 6 |
| Details | binding site for residue MG A 201 |
| Chain | Residue |
| A | SER17 |
| A | GDP202 |
| A | HOH317 |
| A | HOH321 |
| A | HOH331 |
| A | HOH393 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue GDP A 202 |
| Chain | Residue |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| A | ASP30 |
| A | TYR32 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | LEU120 |
| A | SER145 |
| A | ALA146 |
| A | MG201 |
| A | HOH303 |
| A | HOH317 |
| A | HOH321 |
| A | HOH331 |
| A | HOH355 |
| A | HOH378 |
| A | HOH448 |
| A | HOH465 |
| A | HOH514 |
| A | GLY13 |
| A | VAL14 |
| A | GLY15 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ACE A 203 |
| Chain | Residue |
| A | THR2 |
| A | GLU3 |
| A | THR50 |
| A | ALA66 |
| A | HOH380 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | SER17 |
| B | GDP202 |
| B | HOH324 |
| B | HOH328 |
| B | HOH331 |
| B | HOH366 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue GDP B 202 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | GLY15 |
| B | LYS16 |
| B | SER17 |
| B | ALA18 |
| B | ASP30 |
| B | ASN116 |
| B | LYS117 |
| B | ASP119 |
| B | LEU120 |
| B | SER145 |
| B | ALA146 |
| B | LYS147 |
| B | MG201 |
| B | HOH312 |
| B | HOH324 |
| B | HOH328 |
| B | HOH331 |
| B | HOH380 |
| B | HOH398 |
| B | HOH433 |
| B | HOH462 |
| B | HOH467 |
| B | HOH509 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 203 |
| Chain | Residue |
| A | HOH398 |
| B | THR127 |
| B | GLN131 |
| B | PHE141 |
| B | GLU143 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide ACE B 204 and THR B 2 |
| Chain | Residue |
| B | GLU3 |
| B | TYR4 |
| B | CYS51 |
| B | LEU52 |
| B | HOH395 |
| B | HOH439 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Motif: {"description":"Effector region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| 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 | 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
