6HF6

Crystal structure of the Protease 1 (E29A,E60A,E80A) from Pyrococcus horikoshii co-crystallized with Tb-Xo4.

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	0016787	molecular_function	hydrolase 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	0016787	molecular_function	hydrolase 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	0016787	molecular_function	hydrolase activity
C	0036524	molecular_function	protein deglycase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue 7MT A 201

Chain	Residue
A	ALA8
A	ASN9
A	PHE35
A	GLU36
A	ARG75
A	MLI202

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MLI A 202

Chain	Residue
A	ASN9
A	ARG75
A	7MT201

---

site_id	AC3
Number of Residues	2
Details	binding site for residue TB A 204

Chain	Residue
A	GLU10
A	HOH456

---

site_id	AC4
Number of Residues	7
Details	binding site for residue 7MT B 201

Chain	Residue
B	ALA8
B	ASN9
B	PHE35
B	GLU36
B	ARG75
B	MLI202
B	HOH386

---

site_id	AC5
Number of Residues	4
Details	binding site for residue MLI B 202

Chain	Residue
B	ASN9
B	ARG75
B	7MT201
B	HOH386

---

site_id	AC6
Number of Residues	2
Details	binding site for residue TB B 203

Chain	Residue
B	HOH397
B	HOH450

---

site_id	AC7
Number of Residues	6
Details	binding site for residue 7MT C 201

Chain	Residue
C	ALA8
C	ASN9
C	PHE35
C	GLU36
C	ARG75
C	MLI202

---

site_id	AC8
Number of Residues	3
Details	binding site for residue MLI C 202

Chain	Residue
C	ASN9
C	ARG75
C	7MT201

---

site_id	AC9
Number of Residues	3
Details	binding site for residue TB C 203

Chain	Residue
B	HOH417
C	HOH364
C	HOH373

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	495
Details	Domain: {"description":"PfpI endopeptidase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00608","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11114201","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00608","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

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

---