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 | 0005794 | cellular_component | Golgi apparatus |
| A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| A | 0006657 | biological_process | CDP-choline pathway |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| 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 | 0005794 | cellular_component | Golgi apparatus |
| B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| B | 0006657 | biological_process | CDP-choline pathway |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| 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 | 260 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:37179328 |
| Chain | Residue | Details |
| B | MET1-ALA62 | |
| A | SER249-LEU265 | |
| A | MET317-PHE329 | |
| A | LEU377-ASP402 | |
| B | ARG119-SER125 | |
| B | VAL180-ASP190 | |
| B | SER249-LEU265 | |
| B | MET317-PHE329 | |
| B | LEU377-ASP402 | |
| A | MET1-ALA62 | |
| A | ARG119-SER125 | |
| A | VAL180-ASP190 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PRO63-CYS83 | |
| A | PRO63-CYS83 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 98 |
| Details | TOPO_DOM: Lumenal => ECO:0000305|PubMed:37179328 |
| Chain | Residue | Details |
| B | TYR84-PRO93 | |
| A | TYR340-ASP346 | |
| B | VAL151-MET160 | |
| B | CYS208-LEU222 | |
| B | TYR282-ASN293 | |
| B | TYR340-ASP346 | |
| A | TYR84-PRO93 | |
| A | VAL151-MET160 | |
| A | CYS208-LEU222 | |
| A | TYR282-ASN293 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PHE94-ALA118 | |
| A | PHE94-ALA118 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PRO126-ALA150 | |
| A | PRO126-ALA150 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 36 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PHE161-TYR179 | |
| A | PHE161-TYR179 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 32 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | VAL191-VAL207 | |
| A | VAL191-VAL207 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 50 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PRO223-LEU248 | |
| A | PRO223-LEU248 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 30 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | SER266-ILE281 | |
| A | SER266-ILE281 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | PRO294-HIS316 | |
| A | PRO294-HIS316 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | ILE330-GLN339 | |
| A | ILE330-GLN339 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 58 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:37179328 |
| Chain | Residue | Details |
| B | GLU347-HIS376 | |
| A | GLU347-HIS376 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:37179328 |
| Chain | Residue | Details |
| B | HIS133 | |
| A | HIS133 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37179328, ECO:0007744|PDB:8ERP |
| Chain | Residue | Details |
| B | ASN64 | |
| A | ARG119 | |
| A | ASP132 | |
| A | ASP136 | |
| B | ASP111 | |
| B | ASP114 | |
| B | ARG119 | |
| B | ASP132 | |
| B | ASP136 | |
| A | ASN64 | |
| A | ASP111 | |
| A | ASP114 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | SITE: Increases basicity of active site His => ECO:0000305|PubMed:37179328 |
| Chain | Residue | Details |
| B | GLU129 | |
| A | GLU129 |
