Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue H71 A 1001 |
Chain | Residue |
A | ALA123 |
A | TRP231 |
A | THR251 |
A | HOH1111 |
A | ASP158 |
A | ILE161 |
A | GLY162 |
A | MET163 |
A | GLU167 |
A | ASN171 |
A | GLY202 |
A | PHE205 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5XHZ0","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQN1","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |