1E2A
ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 106 |
| Chain | Residue |
| A | ASP81 |
| A | HOH128 |
| A | HOH129 |
| B | ASP81 |
| B | HOH116 |
| C | ASP81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 294 |
| Details | Domain: {"description":"PTS EIIA type-3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00418","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"9261069","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9261069","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphohistidine; by HPr","evidences":[{"source":"PROSITE-ProRule","id":"PRU00418","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9261069","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9261069 |
| Chain | Residue | Details |
| A | HIS78 | |
| A | HIS82 | |
| A | GLN80 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 514 |
| Chain | Residue | Details |
| A | HIS78 | covalent catalysis, electrostatic stabiliser |
| A | GLN80 | electrostatic stabiliser |
| A | HIS82 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 514 |
| Chain | Residue | Details |
| B | HIS78 | covalent catalysis, electrostatic stabiliser |
| B | GLN80 | electrostatic stabiliser |
| B | HIS82 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 514 |
| Chain | Residue | Details |
| C | HIS78 | covalent catalysis, electrostatic stabiliser |
| C | GLN80 | electrostatic stabiliser |
| C | HIS82 | electrostatic stabiliser |
