3EZB
COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI
Replaces: 3EZCReplaces: 3EZDFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
A | 0016310 | biological_process | phosphorylation |
A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
B | 0004857 | molecular_function | enzyme inhibitor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008047 | molecular_function | enzyme activator activity |
B | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
B | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
B | 0030234 | molecular_function | enzyme regulator activity |
B | 0043609 | biological_process | regulation of carbon utilization |
B | 0045152 | molecular_function | antisigma factor binding |
B | 0045819 | biological_process | positive regulation of glycogen catabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00369 |
Number of Residues | 8 |
Details | PTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GLHTRPAA |
Chain | Residue | Details |
B | GLY313-ALA320 |
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 | PS00589 |
Number of Residues | 16 |
Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG |
Chain | Residue | Details |
B | GLY339-GLY354 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
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 | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"33376208","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 84 |
Details | Domain: {"description":"HPr","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"Pros-phosphohistidine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2261470","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1zym |
Chain | Residue | Details |
A | HIS189 | |
A | THR168 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 920 |
Chain | Residue | Details |
A | HIS189 | covalent catalysis |