1J6T
COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | PS00372 |
Number of Residues | 17 |
Details | PTS_EIIA_TYPE_2_HIS PTS EIIA domains phosphorylation site signature 2. EkltptyLGesIAVPHG |
Chain | Residue | Details |
A | GLU50-GLY66 |
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 | 142 |
Details | Domain: {"description":"PTS EIIA type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00417","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Tele-phosphohistidine intermediate; for EIIA activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00417","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12202490","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16443929","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9551558","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Site: {"description":"Stabilizes the transition state in the phosphoryl transfer from HPr to EIIA","evidences":[{"source":"PubMed","id":"9551558","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphohistidine; by HPr","evidences":[{"source":"PubMed","id":"3142516","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12202490","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16443929","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2407724","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9551558","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 84 |
Details | Domain: {"description":"HPr","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
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 |