1CSE

THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0008236	molecular_function	serine-type peptidase activity
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0009611	biological_process	response to wounding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 401

Chain	Residue
E	HOH476
E	ALA169
E	TYR171
E	VAL174
E	HOH402

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 430

Chain	Residue
E	GLN2
E	ASP41
E	LEU75
E	ASN77
E	THR79
E	VAL81

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site_id	ACT
Number of Residues	3
Details	ENZYME CATALYTIC SITE

Chain	Residue
E	ASP32
E	HIS64
E	SER221

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site_id	RSB
Number of Residues	2
Details	INHIBITOR REACTIVE SITE BOND

Chain	Residue
I	LEU45
I	ASP46

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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
E	VAL28-HIS39

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site_id	PS00137
Number of Residues	11
Details	SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA

Chain	Residue	Details
E	HIS64-ALA74

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site_id	PS00138
Number of Residues	11
Details	SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG

Chain	Residue	Details
E	GLY219-GLY229

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site_id	PS00285
Number of Residues	12
Details	POTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA

Chain	Residue	Details
I	PHE10-ALA21

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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	LEU45
E	HIS64
E	SER221

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site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:8512925

Chain	Residue	Details
E	ASN77
E	THR79
E	VAL81
E	ALA169
E	TYR171
E	VAL174
E	GLN2
E	ASP41
E	LEU75

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