Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0051087 | molecular_function | protein-folding chaperone binding |
C | 0005524 | molecular_function | ATP binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
D | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRS A 1382 |
Chain | Residue |
A | ASP10 |
A | HOH2413 |
A | GLY12 |
A | LYS71 |
A | GLU175 |
A | ASP199 |
A | GLY201 |
A | GLY338 |
A | VAL369 |
A | HOH2412 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TRS C 1382 |
Chain | Residue |
C | ASP10 |
C | GLY12 |
C | LYS71 |
C | GLU175 |
C | ASP199 |
C | GLY201 |
C | GLY338 |
C | VAL369 |
C | HOH2021 |
C | HOH2093 |
C | HOH2373 |
C | HOH2381 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TRS C 1383 |
Chain | Residue |
C | ASN256 |
C | ARG258 |
C | ALA259 |
C | ARG262 |
C | SER286 |
C | LEU287 |
C | HOH2271 |
C | HOH2276 |
C | HOH2313 |
C | HOH2382 |
D | LEU218 |
D | GLN245 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRS A 1383 |
Chain | Residue |
A | ASN256 |
A | ARG258 |
A | ALA259 |
A | ARG262 |
A | SER286 |
A | LEU287 |
A | HOH2309 |
A | HOH2314 |
A | HOH2357 |
A | HOH2419 |
B | GLN245 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1384 |
Chain | Residue |
A | GLY201 |
A | GLY202 |
A | LYS271 |
A | GLY339 |
A | SER340 |
A | ASP366 |
A | HOH2265 |
A | HOH2329 |
A | HOH2421 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 1384 |
Chain | Residue |
C | GLY201 |
C | GLY202 |
C | PHE275 |
C | GLY339 |
C | ASP366 |
C | HOH2290 |
C | HOH2353 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 1261 |
Chain | Residue |
B | GLY149 |
B | SER150 |
B | ASN151 |
B | GLU155 |
B | ASN229 |
B | PHE230 |
B | LYS231 |
B | ASP232 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 1261 |
Chain | Residue |
D | ASN151 |
D | GLU155 |
D | ASN229 |
D | PHE230 |
D | LYS231 |
D | ASP232 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 1262 |
Chain | Residue |
A | HIS249 |
A | LYS251 |
B | LEU183 |
B | GLN187 |
B | LEU200 |
B | ASN257 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1385 |
Chain | Residue |
A | ARG171 |
A | GLN376 |
A | ILE379 |
A | LEU380 |
A | HOH2422 |
C | ASP186 |
C | ILE379 |
C | HOH2201 |
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
Chain | Residue | Details |
C | GLY12 | |
C | LYS71 | |
B | SER152 | |
D | SER152 | |
Chain | Residue | Details |
A | GLY202 | |
A | GLU268 | |
A | LYS271 | |
A | PHE275 | |
A | GLY339 | |
C | THR14 | |
C | TYR15 | |
C | GLY202 | |
C | GLU268 | |
C | LYS271 | |
C | PHE275 | |
C | GLY339 | |
A | THR14 | |
A | TYR15 | |
Chain | Residue | Details |
A | SER2 | |
C | SER2 | |
Chain | Residue | Details |
C | LYS108 | |
C | LYS328 | |
A | LYS108 | |
A | LYS328 | |
Chain | Residue | Details |
A | SER153 | |
C | SER153 | |
Chain | Residue | Details |
A | LYS246 | |
C | LYS246 | |
Chain | Residue | Details |
A | LYS319 | |
C | LYS319 | |
Chain | Residue | Details |
A | SER329 | |
C | SER329 | |
Chain | Residue | Details |
A | SER362 | |
C | SER362 | |