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 | 16 |
Details | binding site for residue TI8 A 401 |
Chain | Residue |
A | ASP46 |
A | ASP366 |
A | HOH506 |
A | HOH507 |
A | HOH525 |
A | HOH560 |
A | HOH662 |
A | HOH693 |
A | GLY230 |
A | GLU268 |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY339 |
A | SER340 |
A | ARG342 |
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"}]} |