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 | BET403 |
A | HOH501 |
A | HOH502 |
A | HOH503 |
A | HOH636 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PO4 A 402 |
Chain | Residue |
A | PRO147 |
A | GLU175 |
A | THR204 |
A | MG401 |
A | BET403 |
A | HOH501 |
A | HOH521 |
A | HOH581 |
A | HOH599 |
A | HOH636 |
A | GLY12 |
A | THR13 |
A | LYS71 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BET A 403 |
Chain | Residue |
A | THR13 |
A | THR14 |
A | TYR15 |
A | GLY202 |
A | GLY338 |
A | GLY339 |
A | ASP366 |
A | MG401 |
A | PO4402 |
A | HOH502 |
A | HOH504 |
A | HOH514 |
A | HOH618 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 404 |
Chain | Residue |
A | ARG36 |
A | THR37 |
A | ARG272 |
A | ASN364 |
A | ASP366 |
A | GLU367 |
A | HOH584 |
A | HOH597 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 405 |
Chain | Residue |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY339 |
A | ARG342 |
A | ILE343 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | PO4404 |
B | BET405 |
B | HOH501 |
B | HOH502 |
B | HOH503 |
B | HOH504 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 402 |
Chain | Residue |
B | ARG272 |
B | SER275 |
B | GLY339 |
B | ARG342 |
B | ILE343 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 403 |
Chain | Residue |
B | ARG36 |
B | THR37 |
B | ARG272 |
B | ASN364 |
B | ASP366 |
B | GLU367 |
B | HOH562 |
B | HOH664 |
B | HOH696 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PO4 B 404 |
Chain | Residue |
B | GLY12 |
B | THR13 |
B | LYS71 |
B | PRO147 |
B | GLU175 |
B | THR204 |
B | MG401 |
B | BET405 |
B | HOH503 |
B | HOH504 |
B | HOH629 |
B | HOH640 |
B | HOH641 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BET B 405 |
Chain | Residue |
B | THR13 |
B | THR14 |
B | TYR15 |
B | GLY202 |
B | GLY338 |
B | GLY339 |
B | ASP366 |
B | MG401 |
B | PO4404 |
B | HOH501 |
B | HOH566 |
B | HOH626 |
B | HOH750 |
B | HOH762 |
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 | |
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 | |