1R6V

Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005509	molecular_function	calcium ion binding
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0009986	cellular_component	cell surface
A	0016540	biological_process	protein autoprocessing
A	0019538	biological_process	protein metabolic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	GLU137
A	ASP179
A	LYS219
A	ASP221
A	LYS223
A	ILE225

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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. VAVVDTGVdgtH

Chain	Residue	Details
A	VAL166-HIS177

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

Chain	Residue	Details
A	GLY387-GLY397

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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, ECO:0000305|PubMed:12072953

Chain	Residue	Details
A	ASP170
A	ALA208
A	SER389

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V

Chain	Residue	Details
A	GLU137
A	ASP179
A	ASP221
A	LYS223
A	ILE225
A	LYS219

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