7P5O
Crystal structure of Aspergillus fumigatus phosphoglucomutase in complex with the reaction intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004614 | molecular_function | phosphoglucomutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004614 | molecular_function | phosphoglucomutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00710 |
| Number of Residues | 10 |
| Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIlLTASHNP |
| Chain | Residue | Details |
| A | GLY108-PRO117 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250|UniProtKB:P00949 |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00949 |
| Chain | Residue | Details |
| A | ARG22 | |
| B | ARG22 | |
| B | ASP279 | |
| B | ASP281 | |
| B | ASP283 | |
| B | ARG284 | |
| B | THR347 | |
| B | GLU366 | |
| B | SER368 | |
| B | LYS379 | |
| A | ASP279 | |
| A | ASP281 | |
| A | ASP283 | |
| A | ARG284 | |
| A | THR347 | |
| A | GLU366 | |
| A | SER368 | |
| A | LYS379 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: via phosphate group => ECO:0000250|UniProtKB:P00949 |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P37012 |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 |
