1PSJ
ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS
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 | 0050482 | biological_process | arachidonate secretion |
| A | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 200 |
| Chain | Residue |
| A | TYR28 |
| A | GLY30 |
| A | GLY32 |
| A | ASP49 |
| A | HOH212 |
| site_id | CAL |
| Number of Residues | 4 |
| Details | THE CALCIUM ION IS COORDINATED TO THE TWO CARBOXYLATE OXYGENS OF ASP 49 AND EACH CARBONYL OXYGENS OF TYR 28, GLY 30 AND GLY 32 AS WELL AS TWO WATER MOLECULES (HOH 212 AND HOH 213). THESE LIGAND ATOMS FORM A DISTORTED PENTAGONAL BIPYRAMID STRUCTURE. THE AVERAGE DISTANCE OF CALCIUM ION TO LIGANDS OF PROTEIN OXYGEN IS 2.4 ANGSTROMS. |
| Chain | Residue |
| A | TYR28 |
| A | GLY30 |
| A | GLY32 |
| A | ASP49 |
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":"P06859","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8636969","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9663694","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BK9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PSJ","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 |
