2DP4

Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution

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 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	272
Details	Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {}

Chain

Residue

Details

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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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