2PTC

THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS

Replaces:  1PTC

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 462

Chain	Residue
E	GLU70
E	ASN72
E	VAL75
E	GLU80
E	HOH481
E	HOH559

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Functional Information from PROSITE/UniProt

site_id	PS00280
Number of Residues	19
Details	BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC

Chain	Residue	Details
I	PHE33-CYS51

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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

Chain	Residue	Details
I	LYS15
E	LEU105
E	PRO198

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
E	ILE73
E	VAL75
E	GLY78
E	ILE83
E	GLN192
E	SER195
E	PRO198

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