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 | 0046872 | molecular_function | metal ion binding |
A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
A | 0050482 | biological_process | arachidonate secretion |
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 | 0046872 | molecular_function | metal ion binding |
B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
B | 0050482 | biological_process | arachidonate secretion |
C | 0004623 | molecular_function | phospholipase A2 activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005543 | molecular_function | phospholipid binding |
C | 0005576 | cellular_component | extracellular region |
C | 0006644 | biological_process | phospholipid metabolic process |
C | 0016042 | biological_process | lipid catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
C | 0050482 | biological_process | arachidonate secretion |
Functional Information from PDB Data
site_id | CAA |
Number of Residues | 6 |
Details | CA BINDING SITE. |
Chain | Residue |
A | TYR27 |
A | CYS28 |
A | GLY29 |
A | ARG30 |
A | GLY31 |
A | ASP48 |
site_id | CAB |
Number of Residues | 6 |
Details | CA BINDING SITE. |
Chain | Residue |
B | ARG30 |
B | GLY31 |
B | ASP48 |
B | TYR27 |
B | CYS28 |
B | GLY29 |
site_id | CAC |
Number of Residues | 6 |
Details | CA BINDING SITE. |
Chain | Residue |
C | TYR27 |
C | CYS28 |
C | GLY29 |
C | ARG30 |
C | GLY31 |
C | ASP48 |
Functional Information from PROSITE/UniProt
site_id | PS00118 |
Number of Residues | 8 |
Details | PA2_HIS Phospholipase A2 histidine active site. CCQvHDnC |
Chain | Residue | Details |
A | CYS43-CYS50 | |
site_id | PS00119 |
Number of Residues | 11 |
Details | PA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC |
Chain | Residue | Details |
A | VAL89-CYS99 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS47 | |
A | ASP93 | |
B | HIS47 | |
B | ASP93 | |
C | HIS47 | |
C | ASP93 | |
Chain | Residue | Details |
A | TYR27 | |
C | GLY29 | |
C | GLY31 | |
C | ASP48 | |
A | GLY29 | |
A | GLY31 | |
A | ASP48 | |
B | TYR27 | |
B | GLY29 | |
B | GLY31 | |
B | ASP48 | |
C | TYR27 | |
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 | ASP93 | |
A | GLY29 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
B | HIS47 | |
B | ASP93 | |
B | GLY29 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
C | HIS47 | |
C | ASP93 | |
C | GLY29 | |