5AZB
Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008961 | molecular_function | phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042158 | biological_process | lipoprotein biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS01311 |
| Number of Residues | 13 |
| Details | LGT Prolipoprotein diacylglyceryl transferase signature. GRlGNFINgElwG |
| Chain | Residue | Details |
| A | GLY142-GLY154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 135 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26729647","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AZB","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26729647","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22287519","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 83 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"26729647","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22287519","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26729647","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
