1Y38
Crystal structure of the complex formed between phospholipase A2 dimer and glycerophosphate at 2.4 A resolution
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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | ASP71 |
| A | ARG72 |
| A | GLU92 |
| B | ASP71 |
| B | ARG72 |
| B | GLU92 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | SER70 |
| A | HOH443 |
| A | HOH481 |
| A | ASN67 |
| A | PRO68 |
| A | LYS69 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3P A 201 |
| Chain | Residue |
| A | PHE5 |
| A | ALA18 |
| A | TYR22 |
| A | TRP31 |
| A | CYS45 |
| A | HIS48 |
| A | ASP49 |
| A | HOH476 |
| A | HOH487 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3P B 202 |
| Chain | Residue |
| B | PHE5 |
| B | ALA18 |
| B | TYR22 |
| B | GLY30 |
| B | TRP31 |
| B | CYS45 |
| B | HIS48 |
| B | ASP49 |
| B | HOH573 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PGE B 501 |
| Chain | Residue |
| A | VAL47 |
| A | ALA101 |
| A | CYS105 |
| A | GLN108 |
| A | HOH452 |
| B | SER23 |
| B | SER24 |
| B | GLY30 |
| B | TRP31 |
| B | LEU119 |
| B | TYR120 |
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:P14418 |
| Chain | Residue | Details |
| A | HIS48 | |
| A | ASP99 | |
| B | HIS48 | |
| B | ASP99 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM |
| Chain | Residue | Details |
| A | TYR28 | |
| A | GLY30 | |
| A | GLY32 | |
| A | ASP49 | |
| B | GLY32 | |
| B | ASP49 | |
| B | TYR28 | |
| B | GLY30 |
