5AQF
Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADN A 1382 |
| Chain | Residue |
| A | GLY202 |
| A | ILE343 |
| A | HOH2250 |
| A | HOH2300 |
| A | HOH2384 |
| A | HOH2391 |
| A | GLY230 |
| A | GLU268 |
| A | LYS271 |
| A | ARG272 |
| A | SER275 |
| A | GLY339 |
| A | SER340 |
| A | ARG342 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADN C 1382 |
| Chain | Residue |
| C | GLY202 |
| C | GLY230 |
| C | GLU268 |
| C | LYS271 |
| C | ARG272 |
| C | SER275 |
| C | GLY339 |
| C | SER340 |
| C | ARG342 |
| C | ILE343 |
| C | HOH2207 |
| C | HOH2245 |
| C | HOH2336 |
| C | HOH2342 |
| C | HOH2343 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1383 |
| Chain | Residue |
| A | ASN256 |
| A | ARG258 |
| A | ALA259 |
| A | ARG262 |
| A | SER286 |
| A | LEU287 |
| A | HOH2282 |
| B | GLN245 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1383 |
| Chain | Residue |
| C | ASN256 |
| C | ARG258 |
| C | ALA259 |
| C | ARG262 |
| C | SER286 |
| C | LEU287 |
| D | GLN245 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1262 |
| Chain | Residue |
| A | HIS249 |
| A | LYS251 |
| B | GLN187 |
| B | LEU200 |
| B | ASN257 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1384 |
| Chain | Residue |
| A | GLU27 |
| A | ILE28 |
| A | ALA30 |
| A | ARG36 |
| A | TYR134 |
| A | HOH2038 |
| A | HOH2393 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1385 |
| Chain | Residue |
| A | THR13 |
| A | LYS71 |
| A | ARG76 |
| A | TYR149 |
| A | PHE150 |
| A | HOH2091 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL C 1384 |
| Chain | Residue |
| C | THR13 |
| C | LYS71 |
| C | ARG72 |
| C | ARG76 |
| C | VAL82 |
| C | TYR149 |
| C | PHE150 |
| C | HOH2017 |
| C | HOH2068 |
| C | HOH2071 |
| C | HOH2140 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1263 |
| Chain | Residue |
| B | SER150 |
| B | ASN151 |
| B | GLU155 |
| B | ASN229 |
| B | LYS231 |
| B | ASP232 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1261 |
| Chain | Residue |
| C | GOL1385 |
| D | SER150 |
| D | ASN151 |
| D | GLU155 |
| D | ASN229 |
| D | LYS231 |
| D | ASP232 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1264 |
| Chain | Residue |
| B | ALA246 |
| B | ALA246 |
| B | PHE247 |
| B | GLU250 |
| B | HOH2089 |
| B | HOH2090 |
| B | HOH2092 |
| B | HOH2095 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1265 |
| Chain | Residue |
| B | HOH2096 |
| B | GLN245 |
| B | ALA246 |
| B | GLU250 |
| B | THR253 |
| B | HOH2089 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1386 |
| Chain | Residue |
| A | ILE181 |
| A | ALA182 |
| A | TYR371 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1385 |
| Chain | Residue |
| C | LYS246 |
| C | LYS250 |
| C | LYS251 |
| C | ASP252 |
| D | ASN151 |
| D | ASP232 |
| D | GOL1261 |
| D | HOH2019 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS A 1387 |
| Chain | Residue |
| A | ASP10 |
| A | GLY12 |
| A | LYS71 |
| A | GLU175 |
| A | ASP199 |
| A | VAL369 |
| A | HOH2018 |
| A | HOH2381 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS C 1386 |
| Chain | Residue |
| C | ASP10 |
| C | LYS71 |
| C | GLU175 |
| C | ASP199 |
| C | VAL337 |
| C | GLY338 |
| C | VAL369 |
| C | HOH2069 |
| C | HOH2334 |
| C | HOH2344 |
Functional Information from PROSITE/UniProt
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
| Chain | Residue | Details |
| A | ILE9-SER16 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL |
| Chain | Residue | Details |
| A | ILE197-LEU210 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK |
| Chain | Residue | Details |
| A | ILE334-LYS348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 382 |
| Details | Region: {"description":"Interaction with BAG1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P19120","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Lilla S.","von Kriegsheim A.","Lempens A.","Kolch W.","Bilsland A.E.","Keith W.N."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 160 |
| Details | Domain: {"description":"BAG","evidences":[{"source":"PROSITE-ProRule","id":"PRU00369","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
