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 | 0005524 | molecular_function | ATP binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 587 |
Chain | Residue |
A | ADP486 |
A | VO4491 |
A | NA589 |
A | HOH600 |
A | HOH656 |
A | HOH727 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 687 |
Chain | Residue |
B | HOH712 |
B | HOH803 |
B | HOH840 |
B | ADP486 |
B | VO4491 |
B | NA689 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 589 |
Chain | Residue |
A | ASP10 |
A | TYR15 |
A | ADP486 |
A | MG587 |
A | HOH626 |
A | HOH656 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 590 |
Chain | Residue |
A | ASP199 |
A | THR204 |
A | ASP206 |
A | VO4491 |
A | HOH727 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 689 |
Chain | Residue |
B | ASP10 |
B | TYR15 |
B | ADP486 |
B | MG687 |
B | HOH728 |
B | HOH840 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 690 |
Chain | Residue |
B | ASP199 |
B | THR204 |
B | ASP206 |
B | VO4491 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE VO4 A 491 |
Chain | Residue |
A | GLY12 |
A | THR13 |
A | LYS71 |
A | PRO147 |
A | GLU175 |
A | THR204 |
A | ADP486 |
A | MG587 |
A | NA590 |
A | HOH597 |
A | HOH600 |
A | HOH640 |
A | HOH727 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE VO4 B 491 |
Chain | Residue |
B | GLY12 |
B | THR13 |
B | LYS71 |
B | PRO147 |
B | GLU175 |
B | THR204 |
B | ADP486 |
B | MG687 |
B | NA690 |
B | HOH707 |
B | HOH712 |
B | HOH714 |
B | HOH803 |
B | HOH840 |
site_id | AC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE ADP A 486 |
Chain | Residue |
A | GLY12 |
A | THR13 |
A | THR14 |
A | TYR15 |
A | GLY201 |
A | GLY202 |
A | GLY230 |
A | GLU268 |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY338 |
A | GLY339 |
A | SER340 |
A | ARG342 |
A | ILE343 |
A | ASP366 |
A | VO4491 |
A | MG587 |
A | NA589 |
A | HOH591 |
A | HOH597 |
A | HOH622 |
A | HOH626 |
A | HOH656 |
A | HOH663 |
A | HOH720 |
A | HOH727 |
site_id | BC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE ADP B 486 |
Chain | Residue |
B | GLY338 |
B | GLY339 |
B | SER340 |
B | ARG342 |
B | ILE343 |
B | ASP366 |
B | VO4491 |
B | MG687 |
B | NA689 |
B | HOH701 |
B | HOH707 |
B | HOH712 |
B | HOH728 |
B | HOH799 |
B | HOH824 |
B | HOH829 |
B | HOH840 |
B | GLY12 |
B | THR13 |
B | THR14 |
B | TYR15 |
B | GLY201 |
B | GLY202 |
B | GLY230 |
B | GLU268 |
B | LYS271 |
B | ARG272 |
B | SER275 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 1 |
Chain | Residue |
A | GLU318 |
A | LYS328 |
B | ARG311 |
B | LEU314 |
B | LEU349 |
B | ASP352 |
B | PHE353 |
B | HOH736 |
B | HOH818 |
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 | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY12 | |
A | LYS71 | |
B | GLY12 | |
B | LYS71 | |
Chain | Residue | Details |
A | THR14 | |
B | GLY202 | |
B | GLU268 | |
B | LYS271 | |
B | SER275 | |
B | GLY339 | |
A | TYR15 | |
A | GLY202 | |
A | GLU268 | |
A | LYS271 | |
A | SER275 | |
A | GLY339 | |
B | THR14 | |
B | TYR15 | |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
Chain | Residue | Details |
A | LYS108 | |
A | LYS328 | |
B | LYS108 | |
B | LYS328 | |
Chain | Residue | Details |
A | SER153 | |
A | SER329 | |
A | SER362 | |
B | SER153 | |
B | SER329 | |
B | SER362 | |
Chain | Residue | Details |
A | LYS246 | |
B | LYS246 | |
Chain | Residue | Details |
A | LYS319 | |
B | LYS319 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1kaz |
Chain | Residue | Details |
A | LYS71 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1kaz |
Chain | Residue | Details |
B | LYS71 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 656 |
Chain | Residue | Details |
A | ASP10 | |
A | LYS71 | enhance reactivity |
A | GLU175 | |
A | ASP199 | |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 656 |
Chain | Residue | Details |
B | ASP10 | |
B | LYS71 | enhance reactivity |
B | GLU175 | |
B | ASP199 | |