Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
| E | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLA A 301 |
| Chain | Residue |
| A | GLU148 |
| A | LEU152 |
| A | ARG155 |
| D | ARG183 |
| D | LYS187 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | SER153 |
| A | ARG207 |
| A | HOH412 |
| E | HOH451 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| A | ASN164 |
| B | ARG155 |
| B | ARG172 |
| B | GLU173 |
| C | GLY166 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MLA C 301 |
| Chain | Residue |
| B | HOH420 |
| C | ARG155 |
| C | ALA162 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 302 |
| Chain | Residue |
| B | ARG155 |
| C | ASN164 |
| C | ARG221 |
| C | HOH412 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT D 301 |
| Chain | Residue |
| D | GLN212 |
| D | ASP216 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT E 301 |
| Chain | Residue |
| A | ASN143 |
| A | GLY147 |
| E | LYS151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 243 |
| Details | Domain: {"description":"BAG","evidences":[{"source":"PROSITE-ProRule","id":"PRU00369","evidenceCode":"ECO:0000255"}]} |
