2OYF
Crystal Structure of the complex of phospholipase A2 with indole acetic acid at 1.2 A 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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 1301 |
Chain | Residue |
A | SER1 |
A | LEU3 |
A | ARG72 |
A | HOH2052 |
A | HOH2059 |
A | HOH2061 |
A | HOH2210 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1302 |
Chain | Residue |
A | HOH2058 |
A | HOH2105 |
A | ARG43 |
A | HOH2032 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 1303 |
Chain | Residue |
A | GLU4 |
A | ARG72 |
A | LYS74 |
A | HOH2044 |
A | HOH2061 |
A | HOH2071 |
A | HOH2078 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1304 |
Chain | Residue |
A | SER114 |
A | LYS115 |
A | LYS131 |
A | HOH2098 |
A | HOH2168 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1305 |
Chain | Residue |
A | ASN54 |
A | ARG94 |
A | HOH2192 |
A | HOH2200 |
A | HOH2213 |
A | HOH2220 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IAC A 1001 |
Chain | Residue |
A | LEU2 |
A | ILE19 |
A | GLY30 |
A | LYS69 |
A | ASN111 |
A | HOH2100 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY A 2001 |
Chain | Residue |
A | LYS74 |
A | GLU85 |
A | LYS86 |
A | GLY88 |
A | GLU92 |
A | GLN108 |
A | HOH2119 |
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 |