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 ADP A 401 |
Chain | Residue |
A | THR13 |
A | SER275 |
A | GLY338 |
A | GLY339 |
A | SER340 |
A | ARG342 |
A | ASP366 |
A | PO4402 |
A | MG405 |
A | NA406 |
A | NA407 |
A | THR14 |
A | HOH542 |
A | HOH544 |
A | HOH545 |
A | HOH567 |
A | HOH627 |
A | HOH644 |
A | HOH687 |
A | TYR15 |
A | GLY201 |
A | GLY202 |
A | GLY230 |
A | GLU268 |
A | LYS271 |
A | LYS272 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue PO4 A 402 |
Chain | Residue |
A | GLY12 |
A | THR13 |
A | LYS71 |
A | GLU175 |
A | THR204 |
A | ADP401 |
A | MG405 |
A | NA407 |
A | CL409 |
A | HOH533 |
A | HOH534 |
A | HOH545 |
A | HOH559 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue PO4 A 403 |
Chain | Residue |
A | LEU50 |
A | ILE51 |
A | ALA54 |
A | LYS126 |
A | HOH710 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 404 |
Chain | Residue |
A | GLU304 |
A | SER307 |
A | ASP308 |
A | HOH516 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue MG A 405 |
Chain | Residue |
A | ADP401 |
A | PO4402 |
A | NA406 |
A | HOH533 |
A | HOH545 |
A | HOH559 |
A | HOH567 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue NA A 406 |
Chain | Residue |
A | ASP10 |
A | TYR15 |
A | ADP401 |
A | MG405 |
A | HOH567 |
A | HOH644 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue NA A 407 |
Chain | Residue |
A | GLY202 |
A | GLY203 |
A | THR204 |
A | ADP401 |
A | PO4402 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue EPE A 408 |
Chain | Residue |
A | ASN57 |
A | GLN58 |
A | LEU61 |
A | TYR115 |
A | GLU117 |
A | ARG258 |
A | HOH646 |
A | HOH733 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL A 409 |
Chain | Residue |
A | ASP199 |
A | THR204 |
A | ASP206 |
A | PO4402 |
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. LvLvGGsTRIPkVqK |
Chain | Residue | Details |
A | LEU334-LYS348 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | Binding site: {} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |