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 |
| C | 0000774 | molecular_function | adenyl-nucleotide exchange factor activity |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0000774 | molecular_function | adenyl-nucleotide exchange factor activity |
| D | 0005783 | cellular_component | endoplasmic reticulum |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1 |
| Chain | Residue |
| B | GLY58 |
| B | THR59 |
| B | THR60 |
| B | TYR61 |
| B | GLY246 |
| B | GLY247 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2 |
| Chain | Residue |
| A | GLY246 |
| A | GLY247 |
| A | HOH444 |
| A | HOH452 |
| A | THR59 |
| A | THR60 |
| A | TYR61 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 3 |
| Chain | Residue |
| B | GLU276 |
| B | ASP279 |
| B | GLU313 |
| B | LYS316 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 4 |
| Chain | Residue |
| A | GLU276 |
| A | ASP279 |
| A | GLU313 |
| A | LYS316 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 C 5 |
| Chain | Residue |
| C | HOH60 |
| C | PHE218 |
| C | PRO219 |
| C | ASN220 |
| C | PHE221 |
| C | LYS224 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 6 |
| Chain | Residue |
| C | GLU326 |
| C | HOH434 |
| C | HOH436 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 D 7 |
| Chain | Residue |
| D | PHE218 |
| D | PRO219 |
| D | ASN220 |
| D | LYS224 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 D 8 |
| Chain | Residue |
| D | GLU274 |
| D | ASN277 |
| D | GLU326 |
| D | HOH434 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 1 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 427 |
| Chain | Residue |
| A | LYS68 |
| A | ASN69 |
| A | GLN285 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 1 |
Functional Information from PROSITE/UniProt
| site_id | PS00014 |
| Number of Residues | 4 |
| Details | ER_TARGET Endoplasmic reticulum targeting sequence. RDEL |
| Chain | Residue | Details |
| C | ARG418-LEU421 | |
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
| Chain | Residue | Details |
| A | ILE55-SER62 | |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdvSLL |
| Chain | Residue | Details |
| A | VAL242-LEU255 | |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkVqQ |
| Chain | Residue | Details |
| A | ILE379-GLN393 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 154 |
| Details | Region: {"description":"Nucleotide-binding (NBD)","evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
