2HWG
Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008965 | molecular_function | phosphoenolpyruvate-protein phosphotransferase activity |
| A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| A | 0015764 | biological_process | N-acetylglucosamine transport |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008965 | molecular_function | phosphoenolpyruvate-protein phosphotransferase activity |
| B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| B | 0015764 | biological_process | N-acetylglucosamine transport |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | NEP189 |
| A | ARG358 |
| A | GLU431 |
| A | ASP455 |
| A | OXL903 |
| A | HOH1001 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | ASP455 |
| B | ARG465 |
| B | OXL904 |
| B | HOH1002 |
| B | NEP189 |
| B | ARG358 |
| B | GLU431 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE OXL A 903 |
| Chain | Residue |
| A | NEP189 |
| A | ARG296 |
| A | ARG332 |
| A | MSE429 |
| A | GLU431 |
| A | GLY452 |
| A | THR453 |
| A | ASN454 |
| A | ASP455 |
| A | ARG465 |
| A | CYS502 |
| A | GLY503 |
| A | MG901 |
| A | HOH1001 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OXL B 904 |
| Chain | Residue |
| B | NEP189 |
| B | ARG296 |
| B | ARG332 |
| B | MSE429 |
| B | GLU431 |
| B | GLY452 |
| B | THR453 |
| B | ASN454 |
| B | ASP455 |
| B | ARG465 |
| B | GLY503 |
| B | MG902 |
| B | HOH1002 |
Functional Information from PROSITE/UniProt
| site_id | PS00370 |
| Number of Residues | 12 |
| Details | PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR |
| Chain | Residue | Details |
| A | GLY184-ARG195 |
| site_id | PS00742 |
| Number of Residues | 19 |
| Details | PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR |
| Chain | Residue | Details |
| A | ASP447-ARG465 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"12705838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12705838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P23533","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"33376208","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kc7 |
| Chain | Residue | Details |
| A | CYS502 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kc7 |
| Chain | Residue | Details |
| B | CYS502 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kc7 |
| Chain | Residue | Details |
| A | THR168 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kc7 |
| Chain | Residue | Details |
| B | THR168 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 920 |
| Chain | Residue | Details |
| A | ALA201 | covalent catalysis |
| A | ASN483 | metal ligand |
| A | GLY507 | metal ligand |
| A | ASN566 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 920 |
| Chain | Residue | Details |
| B | ALA201 | covalent catalysis |
| B | ASN483 | metal ligand |
| B | GLY507 | metal ligand |
| B | ASN566 | proton shuttle (general acid/base) |
