2PYC
Crystal structure of a monomeric phospholipase A2 from Russell's viper at 1.5A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004623 | molecular_function | phospholipase A2 activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005543 | molecular_function | phospholipid binding |
A | 0005576 | cellular_component | extracellular region |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006644 | biological_process | phospholipid metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0042130 | biological_process | negative regulation of T cell proliferation |
A | 0046872 | molecular_function | metal ion binding |
A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
A | 0050482 | biological_process | arachidonate secretion |
A | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 1210 |
Chain | Residue |
A | ASP39 |
A | ARG43 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 1211 |
Chain | Residue |
A | TYR22 |
A | ACT1212 |
A | HOH2272 |
A | HOH2317 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 1212 |
Chain | Residue |
A | SER23 |
A | ACT1211 |
A | HOH2267 |
A | HOH2269 |
A | LEU2 |
A | ALA18 |
A | ILE19 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | GLU4 |
A | ARG72 |
A | LYS74 |
A | HOH2102 |
A | HOH2135 |
A | HOH2150 |
A | HOH2160 |
A | HOH2178 |
A | HOH2244 |
A | HOH2248 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | TYR113 |
A | SER114 |
A | LYS115 |
A | LYS131 |
A | HOH2191 |
A | HOH2348 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CCN A 2068 |
Chain | Residue |
A | ALA81 |
A | ILE82 |
A | LYS100 |
A | ILE104 |
A | HOH2106 |
A | HOH2132 |
A | HOH2139 |
A | HOH2143 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of a complex formed between group II phospholipase A2 and aspirin at 1.86 A resolution.","authors":["Singh N.","Jabeen T.","Sharma S.","Bhushan A.","Singh T.P."]}},{"source":"PDB","id":"1TGM","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
A | HIS48 | |
A | GLY30 | |
A | ASP99 |