3QTL
Structural Basis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008236 | molecular_function | serine-type peptidase activity |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008236 | molecular_function | serine-type peptidase activity |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00136 |
Number of Residues | 12 |
Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH |
Chain | Residue | Details |
A | VAL28-HIS39 |
site_id | PS00137 |
Number of Residues | 11 |
Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
Chain | Residue | Details |
A | HIS63-ALA73 |
site_id | PS00138 |
Number of Residues | 11 |
Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
Chain | Residue | Details |
A | GLY218-GLY228 |