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 | 10 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
C | ASN181 | |
D | ASN333 | |
C | ASN215 | |
C | ASN233 | |
C | ASN315 | |
C | ASN333 | |
D | ASN181 | |
D | ASN215 | |
D | ASN233 | |
D | ASN315 | |