1KKM
L.casei HprK/P in complex with B.subtilis P-Ser-HPr
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006109 | biological_process | regulation of carbohydrate metabolic process |
| B | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006109 | biological_process | regulation of carbohydrate metabolic process |
| C | 0000155 | molecular_function | phosphorelay sensor kinase activity |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006109 | biological_process | regulation of carbohydrate metabolic process |
| H | 0005515 | molecular_function | protein binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006351 | biological_process | DNA-templated transcription |
| H | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| H | 0043610 | biological_process | regulation of carbohydrate utilization |
| I | 0005515 | molecular_function | protein binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006351 | biological_process | DNA-templated transcription |
| I | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| I | 0043610 | biological_process | regulation of carbohydrate utilization |
| J | 0005515 | molecular_function | protein binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006351 | biological_process | DNA-templated transcription |
| J | 0009401 | biological_process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
| J | 0043610 | biological_process | regulation of carbohydrate utilization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | SER162 |
| A | GLU204 |
| A | PO4501 |
| H | SEP46 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 402 |
| Chain | Residue |
| B | SER162 |
| B | GLU204 |
| B | HOH550 |
| I | SEP46 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 403 |
| Chain | Residue |
| C | GLU204 |
| C | PO4503 |
| C | HOH543 |
| J | SEP46 |
| C | SER162 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | ASP156 |
| A | SER157 |
| A | GLY158 |
| A | VAL159 |
| A | GLY160 |
| A | LYS161 |
| A | SER162 |
| A | CA401 |
| A | HOH533 |
| H | SEP46 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| B | ASP156 |
| B | SER157 |
| B | GLY158 |
| B | VAL159 |
| B | GLY160 |
| B | LYS161 |
| B | SER162 |
| I | SEP46 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 503 |
| Chain | Residue |
| C | ASP156 |
| C | SER157 |
| C | GLY158 |
| C | VAL159 |
| C | GLY160 |
| C | LYS161 |
| C | SER162 |
| C | CA403 |
| J | SEP46 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. TVNLKSIMGVMSLGIA |
| Chain | Residue | Details |
| H | THR41-ALA56 |
| site_id | PS00369 |
| Number of Residues | 8 |
| Details | PTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GIHARPAT |
| Chain | Residue | Details |
| H | GLY13-THR20 |
| site_id | PS00589 |
| Number of Residues | 16 |
| Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKtVNlKSIMGVMsLG |
| Chain | Residue | Details |
| H | GLY39-GLY54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | Region: {"description":"Important for the catalytic mechanism of both phosphorylation and dephosphorylation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Region: {"description":"Important for the catalytic mechanism of dephosphorylation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Pros-phosphohistidine intermediate; alternate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1549615","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Tele-phosphohistidine; alternate","evidences":[{"source":"PubMed","id":"1549615","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by HPrK/P","evidences":[{"source":"PROSITE-ProRule","id":"PRU00681","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
