3NAS
The crystal structure of beta-phosphoglucomutase from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P71447 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASP7 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P71447 |
| Chain | Residue | Details |
| A | ASP9 | |
| B | ASP9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P71447 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASP7 | |
| B | ASP9 | |
| B | GLY44 | |
| B | ILE45 | |
| B | ARG47 | |
| B | SER116 | |
| B | ARG117 | |
| B | ASN118 | |
| B | ASP170 | |
| A | ASP9 | |
| A | GLY44 | |
| A | ILE45 | |
| A | ARG47 | |
| A | SER116 | |
| A | ARG117 | |
| A | ASN118 | |
| A | ASP170 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000250|UniProtKB:P71447 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASP7 |
