6OB3
Crystal structure of G13D-KRAS (GMPPNP-bound) in complex with GAP-related domain (GRD) of neurofibromin (NF1)
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 | 0043087 | biological_process | regulation of GTPase activity |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0007165 | biological_process | signal transduction |
| C | 0016020 | cellular_component | membrane |
| D | 0043087 | biological_process | regulation of GTPase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue GNP A 201 |
| Chain | Residue |
| A | GLY12 |
| A | ASP30 |
| A | PRO34 |
| A | THR35 |
| A | GLY60 |
| A | GLN61 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | SER145 |
| A | ALA146 |
| A | ASP13 |
| A | LYS147 |
| A | MG202 |
| A | HOH323 |
| A | HOH328 |
| A | HOH329 |
| A | HOH332 |
| A | HOH346 |
| A | HOH364 |
| B | ARG1276 |
| A | VAL14 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | SER17 |
| A | THR35 |
| A | GNP201 |
| A | HOH328 |
| A | HOH332 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 1501 |
| Chain | Residue |
| B | PHE1376 |
| B | PRO1377 |
| B | GLN1378 |
| B | ASN1379 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 1502 |
| Chain | Residue |
| B | HOH1691 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MES B 1503 |
| Chain | Residue |
| B | ASP1248 |
| B | HOH1654 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue MES B 1504 |
| Chain | Residue |
| B | TRP1258 |
| D | GLU1333 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MES B 1505 |
| Chain | Residue |
| B | GLN1336 |
| B | ARG1337 |
| B | LEU1340 |
| B | HOH1604 |
| D | LYS1408 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | binding site for residue GNP C 201 |
| Chain | Residue |
| C | GLY12 |
| C | ASP13 |
| C | VAL14 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| C | VAL29 |
| C | ASP30 |
| C | PRO34 |
| C | THR35 |
| C | GLY60 |
| C | ASN116 |
| C | LYS117 |
| C | ASP119 |
| C | LEU120 |
| C | SER145 |
| C | ALA146 |
| C | LYS147 |
| C | MG202 |
| C | HOH306 |
| C | HOH310 |
| C | HOH311 |
| C | HOH313 |
| C | HOH314 |
| C | HOH315 |
| C | HOH327 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 202 |
| Chain | Residue |
| C | SER17 |
| C | THR35 |
| C | GNP201 |
| C | HOH306 |
| C | HOH314 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 203 |
| Chain | Residue |
| C | ARG68 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MES D 1501 |
| Chain | Residue |
| A | GLN22 |
| A | PHE28 |
| A | LYS147 |
| A | THR148 |
| D | ASP1248 |
| D | HIS1251 |
| D | HOH1639 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MES D 1502 |
| Chain | Residue |
| D | LEU1340 |
| D | PRO1442 |
| D | ASP1445 |
| D | HOH1609 |
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 | 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-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 | 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_FI5 |
| 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_FI6 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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 |
