1TDV
Non-specific binding to phospholipase A2:Crystal structure of the complex of PLA2 with a designed peptide Tyr-Trp-Ala-Ala-Ala-Ala at 1.7A 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
Chain | Residue |
A | SER1 |
A | LEU3 |
A | SER70 |
A | ARG72 |
A | HOH1081 |
A | HOH1106 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
Chain | Residue |
A | HOH1148 |
A | HOH1149 |
A | ARG43 |
A | ARG72 |
A | SO41006 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
Chain | Residue |
A | GLU4 |
A | ARG72 |
A | LYS74 |
A | HOH1081 |
A | HOH1113 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
Chain | Residue |
A | SER90 |
A | ASN93 |
A | HOH1091 |
A | HOH1139 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
Chain | Residue |
A | TYR113 |
A | SER114 |
A | LYS115 |
A | LYS131 |
A | HOH1142 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
Chain | Residue |
A | ASP39 |
A | ARG43 |
A | SO41002 |
A | HOH1079 |
A | HOH1149 |
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 |