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STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004175	molecular_function	endopeptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006508	biological_process	proteolysis
E	0007586	biological_process	digestion
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0097180	cellular_component	serine protease inhibitor complex
E	0097655	molecular_function	serpin family protein binding
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0005576	cellular_component	extracellular region
I	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PROSITE/UniProt

site_id	PS00281
Number of Residues	16
Details	BOWMAN_BIRK Bowman-Birk serine protease inhibitors family signature. CsdirlnSCHSACKSC

Chain	Residue	Details
I	CYS34-CYS49

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site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC

Chain	Residue	Details
E	VAL53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV

Chain	Residue	Details
E	ASP189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond for trypsin => ECO:0000250

Chain	Residue	Details
I	LYS26
E	LEU105
E	PRO198

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Reactive bond for chymotrypsin => ECO:0000250

Chain	Residue	Details
I	TYR53
E	VAL75
E	GLY78
E	ILE83
E	GLN192
E	SER195
E	PRO198

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