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 | 14 |
Details | binding site for residue ADP A 501 |
Chain | Residue |
A | THR63 |
A | ARG391 |
A | ASP414 |
A | PO4502 |
A | MG503 |
A | HOH605 |
A | ASN64 |
A | GLY247 |
A | GLU313 |
A | LYS316 |
A | CYS317 |
A | SER320 |
A | GLY388 |
A | MET389 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 502 |
Chain | Residue |
A | GLY61 |
A | THR62 |
A | LYS121 |
A | GLU222 |
A | THR249 |
A | ASP251 |
A | ADP501 |
A | MG503 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | ASP244 |
A | ADP501 |
A | PO4502 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | TYR196 |
A | ASP251 |
A | THR267 |
A | ASN268 |
A | GLY269 |
A | HOH601 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue ADP B 600 |
Chain | Residue |
B | THR63 |
B | ASN64 |
B | GLY246 |
B | GLY247 |
B | GLU313 |
B | LYS316 |
B | CYS317 |
B | SER320 |
B | GLY387 |
B | GLY388 |
B | MET389 |
B | ARG391 |
B | ASP414 |
B | PO4601 |
B | MG602 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 601 |
Chain | Residue |
B | GLY61 |
B | THR62 |
B | LYS121 |
B | GLU222 |
B | THR249 |
B | ASP251 |
B | ADP600 |
B | MG602 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MG B 602 |
Chain | Residue |
B | ASP244 |
B | ADP600 |
B | PO4601 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKSEDKVIAvyDL |
Chain | Residue | Details |
A | ASP233-LEU245 | |
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS |
Chain | Residue | Details |
A | ILE58-SER65 | |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSIL |
Chain | Residue | Details |
A | VAL242-LEU255 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGmTRMPkVqQ |
Chain | Residue | Details |
A | VAL383-GLN397 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS76 | |
B | LYS76 | |
Chain | Residue | Details |
A | THR87 | |
B | THR87 | |
Chain | Residue | Details |
A | LYS135 | |
A | LYS138 | |
A | LYS206 | |
A | LYS300 | |
B | LYS135 | |
B | LYS138 | |
B | LYS206 | |
B | LYS300 | |
Chain | Residue | Details |
A | LYS143 | |
A | LYS234 | |
A | LYS288 | |
B | LYS143 | |
B | LYS234 | |
B | LYS288 | |
Chain | Residue | Details |
A | LYS368 | |
A | LYS394 | |
B | LYS368 | |
B | LYS394 | |
Chain | Residue | Details |
A | SER408 | |
B | SER408 | |