Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ATP A 486 |
Chain | Residue |
A | GLY12 |
A | GLU268 |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY338 |
A | GLY339 |
A | SER340 |
A | ARG342 |
A | ASP366 |
A | HOH540 |
A | THR13 |
A | HOH551 |
A | HOH573 |
A | HOH584 |
A | HOH585 |
A | HOH635 |
A | HOH697 |
A | HOH702 |
A | THR14 |
A | TYR15 |
A | GLY201 |
A | GLY202 |
A | GLY203 |
A | THR204 |
A | GLY230 |
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 | 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 | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY12 | |
A | LYS71 | |
Chain | Residue | Details |
A | THR14 | |
A | TYR15 | |
A | GLY202 | |
A | GLU268 | |
A | LYS271 | |
A | SER275 | |
A | GLY339 | |
Chain | Residue | Details |
A | LYS108 | |
A | LYS328 | |
Chain | Residue | Details |
A | SER153 | |
A | SER329 | |
A | SER362 | |
Chain | Residue | Details |
A | LYS246 | |
Chain | Residue | Details |
A | 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 | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 656 |
Chain | Residue | Details |
A | ASP10 | |
A | LYS71 | enhance reactivity |
A | GLU175 | |
A | SER199 | |