1GL0

structure of the complex between bovine alpha-chymotrypsin and PMP-D2v, an inhibitor from the insect Locusta migratoria

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
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	0097180	cellular_component	serine protease inhibitor complex
E	0097655	molecular_function	serpin family protein binding
I	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD E1246

Chain	Residue
E	ASP72
E	ASP153
E	ASP178
E	HOH2014

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD E1247

Chain	Residue
E	GLU49
E	ASP128
E	HOH2021
E	HOH2042

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD E1248

Chain	Residue
E	HOH2008
E	ASN245

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Functional Information from PROSITE/UniProt

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

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. SScmGDSGGPLV

Chain	Residue	Details
E	SER189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
I	LEU29
E	ASP102
E	SER195

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
E	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
E	ASP102	modifies pKa
E	GLY193	electrostatic stabiliser
E	SER195	covalent catalysis
E	GLY196	electrostatic stabiliser

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