1IJL
Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus
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 | 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 | arachidonic acid 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 | 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 | arachidonic acid secretion |
B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 201 |
Chain | Residue |
A | HIS33 |
A | HOH247 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 202 |
Chain | Residue |
B | TYR27 |
B | GLY29 |
B | GLY31 |
B | ASP48 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 203 |
Chain | Residue |
A | ASP48 |
A | TYR27 |
A | GLY29 |
A | GLY31 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P00593 |
Chain | Residue | Details |
A | HIS47 | |
A | ASP89 | |
B | HIS47 | |
B | ASP89 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL |
Chain | Residue | Details |
A | TYR27 | |
A | GLY29 | |
A | GLY31 | |
B | TYR27 | |
B | GLY29 | |
B | GLY31 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11752784 |
Chain | Residue | Details |
A | ASP48 | |
B | ASP48 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
A | HIS47 | |
A | ASP89 | |
A | GLY29 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
B | HIS47 | |
B | ASP89 | |
B | GLY29 |