1S6B
X-ray Crystal Structure of a Complex Formed Between Two Homologous Isoforms of Phospholipase A2 from Naja naja sagittifera: Principle of Molecular Association and Inactivation
Replaces: 1LFJFunctional 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 | 0046872 | molecular_function | metal ion binding |
| A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| A | 0050482 | biological_process | arachidonic acid secretion |
| B | 0004623 | molecular_function | phospholipase A2 activity |
| B | 0005102 | molecular_function | signaling receptor binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0048146 | biological_process | positive regulation of fibroblast proliferation |
| B | 0050482 | biological_process | arachidonic acid secretion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 401 |
| Chain | Residue |
| A | ASP24 |
| A | ASN112 |
| A | HOH537 |
| B | ASP24 |
| B | ASN112 |
| B | HOH715 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 402 |
| Chain | Residue |
| B | ASP49 |
| B | PO4501 |
| B | HOH627 |
| B | TYR28 |
| B | GLY30 |
| B | GLY32 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 501 |
| Chain | Residue |
| B | TYR28 |
| B | CYS29 |
| B | GLY30 |
| B | CYS45 |
| B | HIS48 |
| B | ASP49 |
| B | CA402 |
| B | HOH673 |
| B | HOH697 |
| B | HOH799 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | ASN1 |
| A | TYR3 |
| A | GLN65 |
| A | HOH606 |
| B | ASN109 |
| B | HOH731 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY B 601 |
| Chain | Residue |
| B | GLY32 |
| B | HOH674 |
| B | HOH745 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 602 |
| Chain | Residue |
| B | HOH634 |
| B | HOH702 |
| B | HOH718 |
| B | HOH775 |
| B | HOH784 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418 |
| Chain | Residue | Details |
| B | HIS48 | |
| B | ASP94 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15828003, ECO:0007744|PDB:1S6B |
| Chain | Residue | Details |
| B | TYR28 | |
| B | GLY30 | |
| B | GLY32 | |
| B | ASP49 |
