1ZWP
The atomic resolution Crystal structure of the Phospholipase A2 (PLA2) complex with Nimesulide reveals its weaker binding to PLA2
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 | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | GLU4 |
| A | HOH808 |
| A | ARG72 |
| A | LYS74 |
| A | HOH637 |
| A | HOH665 |
| A | HOH686 |
| A | HOH689 |
| A | HOH755 |
| A | HOH779 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ASP39 |
| A | ARG43 |
| A | HOH694 |
| A | HOH715 |
| A | HOH796 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | SER114 |
| A | LYS115 |
| A | LYS131 |
| A | HOH725 |
| A | HOH874 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | ALA81 |
| A | LYS86 |
| A | LYS100 |
| A | HOH657 |
| A | HOH661 |
| A | HOH711 |
| A | HOH824 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NIM A 401 |
| Chain | Residue |
| A | TYR28 |
| A | GLY30 |
| A | TRP31 |
| A | GLY32 |
| A | ASP49 |
| A | LYS69 |
| A | ASN111 |
| A | HOH646 |
| A | HOH667 |
| A | HOH704 |
| A | HOH718 |
| A | HOH785 |
| A | HOH787 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MOH A 601 |
| Chain | Residue |
| A | LEU10 |
| A | HOH760 |
| A | HOH774 |
| A | HOH807 |
| A | HOH885 |
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 |
