General Information of Binding Target of SBP (BTS) (ID: ST00348)
BTS Name
Subtilisin BPN'
Synonyms
EC 3.4.21.62; Alkaline protease; Subtilisin DFE; Subtilisin Novo
BTS Type
Protein
Family
Peptidase S8 family
Gene Name
apr
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Function
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.
UniProt ID
P00782
UniProt Entry
SUBT_BACAM
PFam
PF05922 ; PF00082
Sequence
MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVI
SEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKA
PALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVA
ALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSA
ALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVG
PELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT
TTKLGDSFYYGKGLINVQAAAQ
Sequence Length
382
Synthetic Binding Protein (SBP) Targeting This BTS
SBP Name Highest Status Mechanism Affinity Application Details Ref
CI2-based binder anti-Subtilisin-BPN E60A mutant Research Inhibitor Kd: 0.52 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN E60S mutant Research Inhibitor Kd: 0.31 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN M59R/E60S mutant Research Inhibitor Kd: 1.2 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN R62A mutant Research Inhibitor Kd: 0.025 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN R65A mutant Research Inhibitor Kd: 1.7 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN R67A mutant Research Inhibitor Kd: 0.56 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN T58A mutant Research Inhibitor Kd: 0.3 nM Research tool
SBP Info
[1]
CI2-based binder anti-Subtilisin-BPN T58P mutant Research Inhibitor Kd: 1.7 nM Research tool
SBP Info
[1]
References
1 Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2. Biochemistry. 2005 May 10;44(18):6823-30.