1FW3
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004620 | molecular_function | phospholipase activity |
| A | 0004622 | molecular_function | lysophospholipase activity |
| A | 0004623 | molecular_function | phospholipase A2 activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008970 | molecular_function | phospholipase A1 activity |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046471 | biological_process | phosphatidylglycerol metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052739 | molecular_function | phosphatidylserine 1-acylhydrolase activity |
| A | 0052740 | molecular_function | 1-acyl-2-lysophosphatidylserine acylhydrolase activity |
| B | 0004620 | molecular_function | phospholipase activity |
| B | 0004622 | molecular_function | lysophospholipase activity |
| B | 0004623 | molecular_function | phospholipase A2 activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008970 | molecular_function | phospholipase A1 activity |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046471 | biological_process | phosphatidylglycerol metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052739 | molecular_function | phosphatidylserine 1-acylhydrolase activity |
| B | 0052740 | molecular_function | 1-acyl-2-lysophosphatidylserine acylhydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 90 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| A | GLN1-LEU32 | |
| B | ALA129-GLY130 | |
| B | GLY167-ASN168 | |
| B | GLY204-ASP205 | |
| B | ILE231-VAL235 | |
| B | ASP267-PHE269 | |
| A | GLY80-ASN85 | |
| A | ALA129-GLY130 | |
| A | GLY167-ASN168 | |
| A | GLY204-ASP205 | |
| A | ILE231-VAL235 | |
| A | ASP267-PHE269 | |
| B | GLN1-LEU32 | |
| B | GLY80-ASN85 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 266 |
| Details | TRANSMEM: Beta stranded |
| Chain | Residue | Details |
| A | TYR33-THR45 | |
| A | GLY222-PRO230 | |
| A | ARG236-TYR245 | |
| A | ASN255-ASN266 | |
| B | TYR33-THR45 | |
| B | ASP65-ARG79 | |
| B | SER86-TRP98 | |
| B | PHE109-PHE128 | |
| B | TRP131-S1H144 | |
| B | SER154-ASN166 | |
| B | TRP169-VAL178 | |
| A | ASP65-ARG79 | |
| B | LEU197-LEU203 | |
| B | ALA206-TYR214 | |
| B | GLY222-PRO230 | |
| B | ARG236-TYR245 | |
| B | ASN255-ASN266 | |
| A | SER86-TRP98 | |
| A | PHE109-PHE128 | |
| A | TRP131-S1H144 | |
| A | SER154-ASN166 | |
| A | TRP169-VAL178 | |
| A | LEU197-LEU203 | |
| A | ALA206-TYR214 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 132 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| A | SER46-LYS64 | |
| B | VAL179-GLN196 | |
| B | ASN215-GLY221 | |
| B | GLY246-PHE254 | |
| A | GLN99-PRO108 | |
| A | ASN145-ARG153 | |
| A | VAL179-GLN196 | |
| A | ASN215-GLY221 | |
| A | GLY246-PHE254 | |
| B | SER46-LYS64 | |
| B | GLN99-PRO108 | |
| B | ASN145-ARG153 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305 |
| Chain | Residue | Details |
| A | HIS142 | |
| B | HIS142 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:2040286 |
| Chain | Residue | Details |
| A | S1H144 | |
| B | S1H144 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: in dimeric form |
| Chain | Residue | Details |
| A | SER106 | |
| A | ARG147 | |
| A | SER152 | |
| B | SER106 | |
| B | ARG147 | |
| B | SER152 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: in monomeric form |
| Chain | Residue | Details |
| A | ASP184 | |
| B | ASP184 |
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 | GLY146 | electrostatic stabiliser |
| A | ARG147 | metal ligand |
| A | SER152 | metal ligand |
| A | ASN156 | 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 | GLY146 | electrostatic stabiliser |
| B | ARG147 | metal ligand |
| B | SER152 | metal ligand |
| B | ASN156 | electrostatic stabiliser, increase basicity |
