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 PZA A 1385 |
Chain | Residue |
A | ASN237 |
A | VAL240 |
A | SER241 |
A | GLY256 |
A | VAL262 |
A | ARG266 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PZA B 1385 |
Chain | Residue |
B | GLY256 |
B | ARG266 |
B | HOH2407 |
B | ASN237 |
B | VAL240 |
B | SER241 |
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 | ILE199-LEU212 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK |
Chain | Residue | Details |
A | ILE336-LYS350 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY12 | |
B | GLY341 | |
A | LYS71 | |
A | GLY204 | |
A | GLU270 | |
A | GLY341 | |
B | GLY12 | |
B | LYS71 | |
B | GLY204 | |
B | GLU270 | |