6MQT
HRAS G12S in complex with GDP
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 |
| G | 0003924 | molecular_function | GTPase activity |
| G | 0005525 | molecular_function | GTP binding |
| G | 0007165 | biological_process | signal transduction |
| G | 0016020 | cellular_component | membrane |
| H | 0003924 | molecular_function | GTPase activity |
| H | 0005525 | molecular_function | GTP binding |
| H | 0007165 | biological_process | signal transduction |
| H | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue GDP A 201 |
| Chain | Residue |
| A | GLY13 |
| A | TYR32 |
| A | ASN116 |
| A | LYS117 |
| A | ASP119 |
| A | LEU120 |
| A | SER145 |
| A | ALA146 |
| A | LYS147 |
| A | MG202 |
| A | HOH326 |
| A | VAL14 |
| A | HOH330 |
| A | HOH332 |
| A | HOH346 |
| A | HOH347 |
| A | HOH362 |
| A | HOH400 |
| A | HOH404 |
| A | HOH426 |
| A | GLY15 |
| A | LYS16 |
| A | SER17 |
| A | ALA18 |
| A | PHE28 |
| A | VAL29 |
| A | ASP30 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | SER17 |
| A | GDP201 |
| A | HOH326 |
| A | HOH332 |
| A | HOH347 |
| A | HOH379 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue GDP B 201 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | GLY15 |
| B | LYS16 |
| B | SER17 |
| B | ALA18 |
| B | PHE28 |
| B | VAL29 |
| B | ASP30 |
| B | TYR32 |
| B | ASN116 |
| B | LYS117 |
| B | ASP119 |
| B | LEU120 |
| B | SER145 |
| B | ALA146 |
| B | LYS147 |
| B | MG202 |
| B | HOH318 |
| B | HOH326 |
| B | HOH327 |
| B | HOH345 |
| B | HOH355 |
| B | HOH380 |
| B | HOH392 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | SER17 |
| B | GDP201 |
| B | HOH309 |
| B | HOH318 |
| B | HOH326 |
| B | HOH343 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue GDP C 201 |
| Chain | Residue |
| C | GLY13 |
| C | VAL14 |
| C | GLY15 |
| C | LYS16 |
| C | SER17 |
| C | ALA18 |
| C | PHE28 |
| C | VAL29 |
| C | ASP30 |
| C | TYR32 |
| C | ASN116 |
| C | LYS117 |
| C | ASP119 |
| C | LEU120 |
| C | SER145 |
| C | ALA146 |
| C | LYS147 |
| C | MG202 |
| C | HOH306 |
| C | HOH315 |
| C | HOH324 |
| C | HOH333 |
| C | HOH350 |
| C | HOH378 |
| C | HOH389 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 202 |
| Chain | Residue |
| C | SER17 |
| C | GDP201 |
| C | HOH306 |
| C | HOH307 |
| C | HOH315 |
| C | HOH332 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | binding site for residue GDP D 201 |
| Chain | Residue |
| D | SER17 |
| D | ALA18 |
| D | PHE28 |
| D | VAL29 |
| D | ASP30 |
| D | TYR32 |
| D | ASN116 |
| D | LYS117 |
| D | ASP119 |
| D | LEU120 |
| D | SER145 |
| D | ALA146 |
| D | LYS147 |
| D | MG202 |
| D | HOH314 |
| D | HOH328 |
| D | HOH332 |
| D | HOH337 |
| D | HOH347 |
| D | HOH350 |
| D | HOH373 |
| D | HOH415 |
| D | GLY13 |
| D | VAL14 |
| D | GLY15 |
| D | LYS16 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 202 |
| Chain | Residue |
| D | SER17 |
| D | GDP201 |
| D | HOH332 |
| D | HOH337 |
| D | HOH350 |
| D | HOH359 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | binding site for residue GDP E 201 |
| Chain | Residue |
| E | GLY13 |
| E | VAL14 |
| E | GLY15 |
| E | LYS16 |
| E | SER17 |
| E | ALA18 |
| E | PHE28 |
| E | VAL29 |
| E | ASP30 |
| E | ASN116 |
| E | LYS117 |
| E | ASP119 |
| E | LEU120 |
| E | SER145 |
| E | ALA146 |
| E | LYS147 |
| E | MG202 |
| E | HOH322 |
| E | HOH325 |
| E | HOH334 |
| E | HOH335 |
| E | HOH336 |
| E | HOH345 |
| E | HOH387 |
| E | HOH426 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG E 202 |
| Chain | Residue |
| E | SER17 |
| E | GDP201 |
| E | HOH325 |
| E | HOH335 |
| E | HOH336 |
| E | HOH366 |
| site_id | AD2 |
| Number of Residues | 27 |
| Details | binding site for residue GDP F 201 |
| Chain | Residue |
| E | ARG73 |
| F | GLY13 |
| F | VAL14 |
| F | GLY15 |
| F | LYS16 |
| F | SER17 |
| F | ALA18 |
| F | PHE28 |
| F | VAL29 |
| F | ASP30 |
| F | ASN116 |
| F | LYS117 |
| F | ASP119 |
| F | LEU120 |
| F | SER145 |
| F | ALA146 |
| F | LYS147 |
| F | MG202 |
| F | HOH322 |
| F | HOH331 |
| F | HOH336 |
| F | HOH346 |
| F | HOH351 |
| F | HOH371 |
| F | HOH392 |
| F | HOH402 |
| F | HOH418 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 202 |
| Chain | Residue |
| F | SER17 |
| F | GDP201 |
| F | HOH322 |
| F | HOH336 |
| F | HOH346 |
| F | HOH362 |
| site_id | AD4 |
| Number of Residues | 25 |
| Details | binding site for residue GDP G 201 |
| Chain | Residue |
| G | GLY13 |
| G | VAL14 |
| G | GLY15 |
| G | LYS16 |
| G | SER17 |
| G | ALA18 |
| G | PHE28 |
| G | VAL29 |
| G | ASP30 |
| G | ASN116 |
| G | LYS117 |
| G | ASP119 |
| G | LEU120 |
| G | SER145 |
| G | ALA146 |
| G | LYS147 |
| G | MG202 |
| G | HOH326 |
| G | HOH327 |
| G | HOH336 |
| G | HOH337 |
| G | HOH354 |
| G | HOH364 |
| G | HOH372 |
| G | HOH379 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue MG G 202 |
| Chain | Residue |
| G | SER17 |
| G | GDP201 |
| G | HOH327 |
| G | HOH336 |
| G | HOH337 |
| G | HOH351 |
| site_id | AD6 |
| Number of Residues | 25 |
| Details | binding site for residue GDP H 201 |
| Chain | Residue |
| H | GLY13 |
| H | VAL14 |
| H | GLY15 |
| H | LYS16 |
| H | SER17 |
| H | ALA18 |
| H | PHE28 |
| H | VAL29 |
| H | ASP30 |
| H | ASN116 |
| H | LYS117 |
| H | ASP119 |
| H | LEU120 |
| H | SER145 |
| H | ALA146 |
| H | LYS147 |
| H | MG202 |
| H | HOH610 |
| H | HOH614 |
| H | HOH617 |
| H | HOH639 |
| H | HOH640 |
| H | HOH647 |
| H | HOH656 |
| H | HOH660 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue MG H 202 |
| Chain | Residue |
| H | SER17 |
| H | GDP201 |
| H | HOH614 |
| H | HOH616 |
| H | HOH617 |
| H | HOH628 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 64 |
| Details | Motif: {"description":"Effector region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 136 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16698776","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N-acetylmethionine; in GTPase HRas; 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 | 8 |
| Details | Modified residue: {"description":"N-acetylthreonine; in GTPase HRas, 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 | 8 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"9020151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626575","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9632667","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






