1FV0
FIRST STRUCTURAL EVIDENCE OF THE INHIBITION OF PHOSPHOLIPASE A2 BY ARISTOLOCHIC ACID: CRYSTAL STRUCTURE OF A COMPLEX FORMED BETWEEN PHOSPHOLIPASE A2 AND ARISTOLOCHIC ACID
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 |
| B | 0004623 | molecular_function | phospholipase A2 activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006644 | biological_process | phospholipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042130 | biological_process | negative regulation of T cell proliferation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| B | 0050482 | biological_process | arachidonate secretion |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | SER114 |
| A | LYS115 |
| A | HOH842 |
| A | HOH911 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ALA40 |
| A | ARG43 |
| A | HOH890 |
| A | HOH932 |
| A | HOH968 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| A | ARG77 |
| A | GLY80 |
| B | SER114 |
| B | LYS116 |
| B | HOH799 |
| B | HOH808 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | LYS38 |
| B | ASP39 |
| B | ARG43 |
| B | HOH765 |
| B | HOH791 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 801 |
| Chain | Residue |
| A | ASN67 |
| A | LYS69 |
| A | SER70 |
| B | LEU130 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 9AR A 401 |
| Chain | Residue |
| A | LEU2 |
| A | PHE5 |
| A | ILE9 |
| A | ALA18 |
| A | ILE19 |
| A | TYR22 |
| A | GLY30 |
| A | TRP31 |
| A | CYS45 |
| A | HIS48 |
| A | ASP49 |
| A | LYS69 |
| A | HOH971 |
| B | PHE46 |
| B | VAL47 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DIO B 701 |
| Chain | Residue |
| B | ARG107 |
| B | LEU110 |
| B | ASN111 |
| B | DIO702 |
| B | DIO702 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIO B 702 |
| Chain | Residue |
| A | PHE124 |
| B | GLN108 |
| B | ASN111 |
| B | DIO701 |
| B | DIO701 |
| B | HOH736 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 601 |
| Chain | Residue |
| A | PRO121 |
| A | HOH892 |
| B | GLU11 |
| B | GLU12 |
| B | HOH804 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 602 |
| Chain | Residue |
| A | LYS38 |
| A | LYS116 |
| A | TYR117 |
| A | HOH956 |
| B | GLU11 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| 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 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| B | HIS48 | |
| B | GLY30 | |
| B | ASP99 |
