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 | 17 |
| Details | binding site for residue AMP A 501 |
| Chain | Residue |
| A | ASN64 |
| A | GLY388 |
| A | MET389 |
| A | ARG391 |
| A | ASP414 |
| A | PIS502 |
| A | HOH602 |
| A | HOH606 |
| A | HOH678 |
| A | GLY246 |
| A | GLY247 |
| A | GLY275 |
| A | GLU313 |
| A | LYS316 |
| A | CYS317 |
| A | SER320 |
| A | GLY387 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue PIS A 502 |
| Chain | Residue |
| A | ASP59 |
| A | GLY61 |
| A | THR62 |
| A | LYS121 |
| A | GLU222 |
| A | ASP244 |
| A | THR249 |
| A | AMP501 |
| A | HOH602 |
| A | HOH641 |
| A | HOH667 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ARG85 |
| A | ARG391 |
| A | ASN412 |
| A | ASP414 |
| A | GLU415 |
| A | HOH665 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30933555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NHK","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
