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 |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue ANP A 300 |
| Chain | Residue |
| A | ASN119 |
| A | THR251 |
| A | MG301 |
| A | HOH422 |
| A | HOH424 |
| A | HOH429 |
| A | HOH430 |
| A | HOH431 |
| A | HOH433 |
| A | HOH442 |
| A | HOH443 |
| A | ALA123 |
| A | HOH447 |
| A | HOH455 |
| A | HOH458 |
| A | HOH468 |
| A | HOH471 |
| A | HOH474 |
| A | HOH478 |
| A | HOH492 |
| A | HOH498 |
| A | HOH523 |
| A | LYS126 |
| A | ASP158 |
| A | MET163 |
| A | ASN171 |
| A | ARG177 |
| A | GLY204 |
| A | PHE205 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASN119 |
| A | ANP300 |
| A | HOH443 |
| A | HOH458 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | binding site for residue ANP B 300 |
| Chain | Residue |
| B | ASN119 |
| B | ALA123 |
| B | LYS126 |
| B | ASP158 |
| B | MET163 |
| B | ASN171 |
| B | ARG177 |
| B | GLY204 |
| B | PHE205 |
| B | THR251 |
| B | MG301 |
| B | HOH427 |
| B | HOH431 |
| B | HOH440 |
| B | HOH442 |
| B | HOH444 |
| B | HOH449 |
| B | HOH453 |
| B | HOH462 |
| B | HOH469 |
| B | HOH483 |
| B | HOH485 |
| B | HOH496 |
| B | HOH513 |
| B | HOH522 |
| B | HOH533 |
| B | HOH552 |
| B | HOH554 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASN119 |
| B | ANP300 |
| B | HOH469 |
| B | HOH513 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5XHZ0","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q5XHZ0","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQN1","evidenceCode":"ECO:0000250"}]} |
