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	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	0016787	molecular_function	hydrolase activity
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

---

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

---

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

Chain	Residue	Details
A	GLY387-GLY397

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	302
Details	Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

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"},{"source":"PubMed","id":"12072953","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14687574","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R6V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---