1BJR

COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 290

Chain	Residue
E	ARG12
E	SER15
E	ASN257
E	ALA273
E	TYR274

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA E 291

Chain	Residue
E	HOH396
E	HOH433
E	HOH447
E	PRO175
E	VAL177
E	ASP200
E	HOH363

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site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR CHAIN I OF LACTOFERRIN

Chain	Residue
E	THR40
E	ASN67
E	HIS69
E	LEU96
E	ASP98
E	ASN99
E	GLY100
E	SER132
E	LEU133
E	GLY134
E	GLY135
E	VAL157
E	ALA158
E	ALA159
E	GLY160
E	ASN161
E	ASN162
E	TYR169
E	PRO171
E	ALA172
E	ASN194
E	TRP212
E	ILE220
E	GLY222
E	THR223
E	SER224
E	MET225
E	SER247
E	ARG250
E	HOH339
I	HOH349

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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. VYVIDTGIeasH

Chain	Residue	Details
E	VAL35-HIS46

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

Chain	Residue	Details
E	HIS69-SER79

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

Chain	Residue	Details
E	GLY222-GLY232

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240

Chain	Residue	Details
E	ASP39
E	HIS69
E	SER224

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
E	THR16
E	PRO175
E	VAL177
E	ASP200
E	ASP260

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1sca

Chain	Residue	Details
E	SER224
E	ASP39
E	HIS69

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