Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004620 | molecular_function | phospholipase activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016020 | cellular_component | membrane |
| D | 0004620 | molecular_function | phospholipase activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 1 |
| Chain | Residue |
| C | ARG147 |
| C | SER152 |
| C | HOH285 |
| C | HOH294 |
| D | SER106 |
| D | HOH275 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 2 |
| Chain | Residue |
| D | HOH302 |
| C | SER106 |
| D | ARG147 |
| D | SER152 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HDS C 270 |
| Chain | Residue |
| C | TYR92 |
| C | TYR114 |
| C | HIS142 |
| C | SER144 |
| C | ASN145 |
| C | GLY146 |
| C | HOH285 |
| D | TYR39 |
| D | PHE69 |
| D | TRP98 |
| D | PHE109 |
| D | VAL263 |
| D | LEU265 |
| D | HOH275 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HDS D 270 |
| Chain | Residue |
| C | TYR39 |
| C | LEU71 |
| C | TRP98 |
| C | PHE109 |
| C | VAL263 |
| C | LEU265 |
| D | TYR92 |
| D | HIS142 |
| D | SER144 |
| D | ASN145 |
| D | GLY146 |
| D | HOH302 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Transmembrane: {"description":"Beta stranded"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | Topological domain: {"description":"Extracellular"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Periplasmic"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"2040286","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in dimeric form"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in monomeric form"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8575454, 2040286, 8672479, 10537112 |
| Chain | Residue | Details |
| D | GLY146 | |
| C | HIS142 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 650 |
| Chain | Residue | Details |
| C | SER106 | metal ligand |
| C | HIS142 | proton acceptor, proton donor |
| C | SER144 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | GLY146 | electrostatic stabiliser |
| C | ARG147 | metal ligand |
| C | SER152 | metal ligand |
| C | ASN156 | electrostatic stabiliser, increase basicity |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 650 |
| Chain | Residue | Details |
| D | SER106 | metal ligand |
| D | HIS142 | proton acceptor, proton donor |
| D | SER144 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | GLY146 | electrostatic stabiliser |
| D | ARG147 | metal ligand |
| D | SER152 | metal ligand |
| D | ASN156 | electrostatic stabiliser, increase basicity |
