8ERP
Structure of Xenopus cholinephosphotransferase1 in complex with CDP-choline
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0004142 | molecular_function | diacylglycerol cholinephosphotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| A | 0006657 | biological_process | CDP-choline pathway |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0012505 | cellular_component | endomembrane system |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0004142 | molecular_function | diacylglycerol cholinephosphotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| B | 0006657 | biological_process | CDP-choline pathway |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0012505 | cellular_component | endomembrane system |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GlhIglvLLLalMIYkKSTtnLflqnpClY |
| Chain | Residue | Details |
| B | GLY268-TYR297 |
| site_id | PS00379 |
| Number of Residues | 23 |
| Details | CDP_ALCOHOL_P_TRANSF CDP-alcohol phosphatidyltransferases signature. DGkqARrtnsssplGemfDhgcD |
| Chain | Residue | Details |
| B | ASP114-ASP136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 98 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 88 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 58 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ERP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Site: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"37179328","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
