1FW3
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004620 | molecular_function | glycerophospholipase activity |
| A | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| A | 0004623 | molecular_function | A2-type glycerophospholipase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008970 | molecular_function | glycerophospholipid phospholipase A1 activity |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046471 | biological_process | phosphatidylglycerol metabolic process |
| B | 0004620 | molecular_function | glycerophospholipase activity |
| B | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| B | 0004623 | molecular_function | A2-type glycerophospholipase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008970 | molecular_function | glycerophospholipid phospholipase A1 activity |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046471 | biological_process | phosphatidylglycerol metabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 244 |
| Details | Transmembrane: {"description":"Beta stranded"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | Topological domain: {"description":"Extracellular"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Topological domain: {"description":"Periplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"2040286","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in dimeric form"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in monomeric form"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qd6 |
| Chain | Residue | Details |
| A | HIS142 | |
| A | S1H144 | |
| A | GLY146 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qd6 |
| Chain | Residue | Details |
| B | HIS142 | |
| B | S1H144 | |
| B | GLY146 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 650 |
| Chain | Residue | Details |
| A | SER106 | metal ligand |
| A | HIS142 | proton acceptor, proton donor |
| A | S1H144 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | PRO150 | electrostatic stabiliser |
| A | THR151 | metal ligand |
| A | ASN156 | metal ligand |
| A | THR160 | electrostatic stabiliser, increase basicity |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 650 |
| Chain | Residue | Details |
| B | SER106 | metal ligand |
| B | HIS142 | proton acceptor, proton donor |
| B | S1H144 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | PRO150 | electrostatic stabiliser |
| B | THR151 | metal ligand |
| B | ASN156 | metal ligand |
| B | THR160 | electrostatic stabiliser, increase basicity |
