7QO8

Structure of Protease1 from Pyrococcus horikoshii in space group 19 with a hexamer in the asymmetric unit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0036524	molecular_function	protein deglycase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0036524	molecular_function	protein deglycase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0036524	molecular_function	protein deglycase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0036524	molecular_function	protein deglycase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0036524	molecular_function	protein deglycase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0036524	molecular_function	protein deglycase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:11114201

Chain	Residue	Details
A	CYS100
B	CYS100
C	CYS100
D	CYS100
E	CYS100
F	CYS100

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00608

Chain	Residue	Details
A	HIS101
B	HIS101
C	HIS101
D	HIS101
E	HIS101
F	HIS101

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
A	GLY70	electrostatic stabiliser
A	ARG71	electrostatic stabiliser
A	GLU74	electrostatic stabiliser, modifies pKa
A	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	HIS101	electrostatic stabiliser, proton acceptor, proton donor
A	TYR120	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
B	GLY70	electrostatic stabiliser
B	ARG71	electrostatic stabiliser
B	GLU74	electrostatic stabiliser, modifies pKa
B	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
B	HIS101	electrostatic stabiliser, proton acceptor, proton donor
B	TYR120	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
C	GLY70	electrostatic stabiliser
C	ARG71	electrostatic stabiliser
C	GLU74	electrostatic stabiliser, modifies pKa
C	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
C	HIS101	electrostatic stabiliser, proton acceptor, proton donor
C	TYR120	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
D	GLY70	electrostatic stabiliser
D	ARG71	electrostatic stabiliser
D	GLU74	electrostatic stabiliser, modifies pKa
D	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
D	HIS101	electrostatic stabiliser, proton acceptor, proton donor
D	TYR120	electrostatic stabiliser

---

site_id	MCSA5
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
E	GLY70	electrostatic stabiliser
E	ARG71	electrostatic stabiliser
E	GLU74	electrostatic stabiliser, modifies pKa
E	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
E	HIS101	electrostatic stabiliser, proton acceptor, proton donor
E	TYR120	electrostatic stabiliser

---

site_id	MCSA6
Number of Residues	6
Details	M-CSA 964

Chain	Residue	Details
F	GLY70	electrostatic stabiliser
F	ARG71	electrostatic stabiliser
F	GLU74	electrostatic stabiliser, modifies pKa
F	CYS100	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
F	HIS101	electrostatic stabiliser, proton acceptor, proton donor
F	TYR120	electrostatic stabiliser

---