1PP2
THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0004623 | molecular_function | phospholipase A2 activity |
| L | 0005509 | molecular_function | calcium ion binding |
| L | 0005543 | molecular_function | phospholipid binding |
| L | 0005576 | cellular_component | extracellular region |
| L | 0006644 | biological_process | phospholipid metabolic process |
| L | 0016042 | biological_process | lipid catabolic process |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0035821 | biological_process | modulation of process of another organism |
| L | 0042130 | biological_process | negative regulation of T cell proliferation |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| L | 0050482 | biological_process | arachidonic acid secretion |
| L | 0090729 | molecular_function | toxin activity |
| R | 0004623 | molecular_function | phospholipase A2 activity |
| R | 0005509 | molecular_function | calcium ion binding |
| R | 0005543 | molecular_function | phospholipid binding |
| R | 0005576 | cellular_component | extracellular region |
| R | 0006644 | biological_process | phospholipid metabolic process |
| R | 0016042 | biological_process | lipid catabolic process |
| R | 0016787 | molecular_function | hydrolase activity |
| R | 0035821 | biological_process | modulation of process of another organism |
| R | 0042130 | biological_process | negative regulation of T cell proliferation |
| R | 0046872 | molecular_function | metal ion binding |
| R | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| R | 0050482 | biological_process | arachidonic acid secretion |
| R | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | ANL |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE ACTIVATION NETWORK |
| Chain | Residue |
| L | SER1 |
| L | GLN4 |
| L | VAL71 |
| L | TYR73 |
| site_id | ANR |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE ACTIVATION NETWORK |
| Chain | Residue |
| R | SER1 |
| R | GLN4 |
| R | VAL71 |
| R | TYR73 |
| site_id | CAL |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE CA2+ BINDING SITE DEDUCED FROM BOVINE STRUCTURE |
| Chain | Residue |
| L | TYR28 |
| L | GLY30 |
| L | GLY32 |
| L | ASP49 |
| site_id | CAR |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE CA2+ BINDING SITE DEDUCED FROM BOVINE STRUCTURE |
| Chain | Residue |
| R | GLY30 |
| R | GLY32 |
| R | ASP49 |
| R | TYR28 |
| site_id | CNL |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE CATALYTIC NETWORK |
| Chain | Residue |
| L | HIS48 |
| L | TYR52 |
| L | TYR73 |
| L | ASP99 |
| site_id | CNR |
| Number of Residues | 4 |
| Details | RESIDUES FORMING THE CATALYTIC NETWORK |
| Chain | Residue |
| R | HIS48 |
| R | TYR52 |
| R | TYR73 |
| R | ASP99 |
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:0000305|PubMed:4019493 |
| Chain | Residue | Details |
| R | SER72 | |
| R | ASN115 | |
| L | SER72 | |
| L | ASN115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O42191 |
| Chain | Residue | Details |
| R | CYS44 | |
| R | PHE46 | |
| R | HIS48 | |
| R | TYR73 | |
| L | CYS44 | |
| L | PHE46 | |
| L | HIS48 | |
| L | TYR73 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| R | HIS48 | |
| R | GLY30 | |
| R | ASP99 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| L | HIS48 | |
| L | GLY30 | |
| L | ASP99 |
