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 401 |
Chain | Residue |
A | PO4402 |
A | ADP403 |
A | HOH512 |
A | HOH516 |
A | HOH555 |
A | HOH562 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue PO4 A 402 |
Chain | Residue |
A | GLU175 |
A | THR204 |
A | MG401 |
A | ADP403 |
A | HOH508 |
A | HOH523 |
A | HOH555 |
A | HOH562 |
A | GLY12 |
A | THR13 |
A | LYS71 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue ADP A 403 |
Chain | Residue |
A | THR13 |
A | THR14 |
A | TYR15 |
A | GLY201 |
A | GLY202 |
A | GLU268 |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY338 |
A | GLY339 |
A | SER340 |
A | ARG342 |
A | ASP366 |
A | MG401 |
A | PO4402 |
A | HOH501 |
A | HOH505 |
A | HOH508 |
A | HOH516 |
A | HOH531 |
A | HOH553 |
A | HOH555 |
A | HOH562 |
A | HOH581 |
A | HOH597 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ARG311 |
A | LEU314 |
A | LEU349 |
A | PHE353 |
A | GOL405 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ASP315 |
A | GLU318 |
A | GOL404 |
B | ARG311 |
B | LEU349 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | PO4402 |
B | ADP403 |
B | HOH516 |
B | HOH535 |
B | HOH540 |
B | HOH567 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue PO4 B 402 |
Chain | Residue |
B | GLY12 |
B | THR13 |
B | LYS71 |
B | GLU175 |
B | THR204 |
B | ASP206 |
B | MG401 |
B | ADP403 |
B | HOH510 |
B | HOH540 |
B | HOH567 |
site_id | AC8 |
Number of Residues | 23 |
Details | binding site for residue ADP B 403 |
Chain | Residue |
B | THR14 |
B | TYR15 |
B | GLY201 |
B | GLY202 |
B | GLU268 |
B | LYS271 |
B | ARG272 |
B | SER275 |
B | GLY338 |
B | GLY339 |
B | SER340 |
B | ARG342 |
B | ILE343 |
B | MG401 |
B | PO4402 |
B | HOH501 |
B | HOH510 |
B | HOH516 |
B | HOH522 |
B | HOH535 |
B | HOH547 |
B | HOH596 |
B | HOH626 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | HOH518 |
A | ALA307 |
A | ASP308 |
A | ARG311 |
B | ASP308 |
B | GLY312 |
B | ASP315 |
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 | LYS108 | |
A | LYS328 | |
B | LYS108 | |
B | LYS328 | |
Chain | Residue | Details |
A | SER153 | |
B | SER153 | |
Chain | Residue | Details |
A | LYS246 | |
B | LYS246 | |
Chain | Residue | Details |
A | LYS319 | |
B | LYS319 | |
Chain | Residue | Details |
A | SER329 | |
B | SER329 | |
Chain | Residue | Details |
A | SER362 | |
B | SER362 | |