1CM2
STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004857 | molecular_function | enzyme inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| A | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
| A | 0018106 | biological_process | peptidyl-histidine phosphorylation |
| A | 0030234 | molecular_function | enzyme regulator activity |
| A | 0043609 | biological_process | regulation of carbon utilization |
| A | 0045152 | molecular_function | antisigma factor binding |
| A | 0045819 | biological_process | positive regulation of glycogen catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00589 |
| Number of Residues | 16 |
| Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKsASaKSLFKLQtLG |
| Chain | Residue | Details |
| A | GLY39-GLY54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | Domain: {"description":"HPr","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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 |






