3PDK
crystal structure of phosphoglucosamine mutase from B. anthracis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004615 | molecular_function | phosphomannomutase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008966 | molecular_function | phosphoglucosamine mutase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic 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 | 0004615 | molecular_function | phosphomannomutase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0008966 | molecular_function | phosphoglucosamine mutase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 449 |
| Chain | Residue |
| A | VAL306 |
| A | ARG410 |
| A | SER412 |
| A | ARG419 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 450 |
| Chain | Residue |
| A | ASP308 |
| A | MET312 |
| A | HIS329 |
| A | THR338 |
| A | GLY339 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 451 |
| Chain | Residue |
| A | HIS277 |
| A | HOH459 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 449 |
| Chain | Residue |
| B | ARG410 |
| B | SER412 |
| B | THR414 |
| B | ARG419 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 450 |
| Chain | Residue |
| A | THR202 |
| A | MET203 |
| A | GLY204 |
| A | THR205 |
| A | SER206 |
| B | GLY364 |
| B | THR367 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 451 |
| Chain | Residue |
| B | ASP308 |
| B | MET312 |
| B | HIS329 |
| B | ILE331 |
| B | THR338 |
| B | GLY339 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 452 |
| Chain | Residue |
| B | HIS277 |
| B | HOH461 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 453 |
| Chain | Residue |
| B | HIS101 |
| B | ASN102 |
| B | PRO103 |
| B | THR219 |
Functional Information from PROSITE/UniProt
| site_id | PS00710 |
| Number of Residues | 10 |
| Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmISASHNP |
| Chain | Residue | Details |
| A | GLY94-PRO103 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01554","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via phosphate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01554","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01554","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"HAMAP-Rule","id":"MF_01554","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
