1G0Z
SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 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 | 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 | 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 | 3 |
Details | BINDING SITE FOR RESIDUE CL B 121 |
Chain | Residue |
B | THR82 |
B | SER83 |
B | HOH186 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 121 |
Chain | Residue |
A | THR82 |
A | SER83 |
A | HOH167 |
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 | ASP94 | |
B | HIS48 | |
B | ASP94 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14418 |
Chain | Residue | Details |
A | TYR28 | |
A | GLY30 | |
A | GLY32 | |
A | ASP49 | |
B | TYR28 | |
B | GLY30 | |
B | GLY32 | |
B | ASP49 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15721580 |
Chain | Residue | Details |
A | TYR31 | |
B | TYR31 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
A | HIS48 | |
A | GLY30 | |
A | ASP94 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1n29 |
Chain | Residue | Details |
B | HIS48 | |
B | GLY30 | |
B | ASP94 |