5JWY
Structure of lipid phosphate phosphatase PgpB complex with PE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000810 | molecular_function | diacylglycerol diphosphate phosphatase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006655 | biological_process | phosphatidylglycerol biosynthetic process |
| A | 0008195 | molecular_function | phosphatidate phosphatase activity |
| A | 0008962 | molecular_function | phosphatidylglycerophosphatase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0009395 | biological_process | phospholipid catabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| A | 0050380 | molecular_function | undecaprenyl-diphosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue 46E A 301 |
| Chain | Residue |
| A | GLN50 |
| A | VAL88 |
| A | GLY89 |
| A | LYS93 |
| A | PRO160 |
| A | PHE166 |
| A | SER169 |
| A | TRP170 |
| A | LEU222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 95 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"24821770","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24821770","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24821770","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Region: {"description":"Phosphatase sequence motif I","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Region: {"description":"Phosphatase sequence motif II","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor; for a subset of substrates","evidences":[{"source":"PubMed","id":"27405756","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"27405756","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Stabilizes the active site histidine for nucleophilic attack","evidences":[{"source":"PubMed","id":"27405756","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
