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: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP9 | |
| B | ASP9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP7 | |
| A | SER50 | |
| A | LYS76 | |
| A | SER114 | |
| A | LYS145 | |
| A | GLU169 | |
| A | ASP170 | |
| B | ASP7 | |
| B | ASP9 | |
| B | TRP23 | |
| B | LEU42 | |
| B | SER50 | |
| B | LYS76 | |
| B | SER114 | |
| B | LYS145 | |
| B | GLU169 | |
| B | ASP170 | |
| A | ASP9 | |
| A | TRP23 | |
| A | LEU42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups => ECO:0000250 |
| Chain | Residue | Details |
| B | SER114 | |
| B | LYS145 | |
| A | SER114 | |
| A | LYS145 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASP7 |
