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 |
A | 0071704 | biological_process | organic substance metabolic process |
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 |
B | 0071704 | biological_process | organic substance metabolic process |
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 | ACT_SITE: Phosphoserine intermediate => ECO:0000255|HAMAP-Rule:MF_01554 |
Chain | Residue | Details |
A | SER100 | |
B | SER100 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: via phosphate group => ECO:0000255|HAMAP-Rule:MF_01554 |
Chain | Residue | Details |
A | SER100 | |
B | SER100 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01554 |
Chain | Residue | Details |
A | ASP240 | |
A | ASP242 | |
A | ASP244 | |
B | ASP240 | |
B | ASP242 | |
B | ASP244 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_01554 |
Chain | Residue | Details |
A | SER100 | |
B | SER100 |