6V6F
Crystal structure of Q61L KRAS(GMPPNP)-NF1(GRD)-SPRED1(EVH1) complex
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue ZN A 201 |
Chain | Residue |
A | HIS49 |
A | CYS55 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue FMT A 202 |
Chain | Residue |
A | ARG110 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue FMT B 1601 |
Chain | Residue |
B | LYS1419 |
C | GLN70 |
site_id | AC4 |
Number of Residues | 24 |
Details | binding site for residue GNP C 501 |
Chain | Residue |
C | SER17 |
C | ALA18 |
C | PHE28 |
C | VAL29 |
C | ASP30 |
C | GLU31 |
C | TYR32 |
C | PRO34 |
C | THR35 |
C | GLY60 |
C | ASN116 |
C | LYS117 |
C | ASP119 |
C | LEU120 |
C | SER145 |
C | ALA146 |
C | LYS147 |
C | MG502 |
C | HOH603 |
C | HOH604 |
C | GLY13 |
C | VAL14 |
C | GLY15 |
C | LYS16 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | SER17 |
C | THR35 |
C | ASP57 |
C | GNP501 |
C | HOH603 |
C | HOH604 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue FMT C 503 |
Chain | Residue |
C | TYR137 |
Functional Information from PROSITE/UniProt
site_id | PS00509 |
Number of Residues | 15 |
Details | RAS_GTPASE_ACTIV_1 Ras GTPase-activating proteins (rasGAP) domain signature. SaMFLRFINPAIVSP |
Chain | Residue | Details |
B | SER1386-PRO1400 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Site: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00167","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Motif: {"description":"Effector region"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
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_FI4 |
Number of Residues | 1 |
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_FI5 |
Number of Residues | 1 |
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_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
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 |