6F2F

Crystal structure of Protease 1 from Pyrococcus Horikoshii co-cystallized in presence of 10 mM Tb-Xo4 and ammonium sulfate.

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	SO4202

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 202

Chain	Residue
A	HOH362
A	ASN9
A	ARG75
A	7MT201

---

site_id	AC3
Number of Residues	1
Details	binding site for residue SO4 A 203

Chain	Residue
A	ARG149

---

site_id	AC4
Number of Residues	2
Details	binding site for residue TB A 204

Chain	Residue
A	HOH441
B	HOH474

---

site_id	AC5
Number of Residues	6
Details	binding site for residue 7MT B 201

Chain	Residue
B	ALA8
B	ASN9
B	PHE35
B	GLU36
B	ARG75
B	SO4204

---

site_id	AC6
Number of Residues	1
Details	binding site for residue SO4 B 202

Chain	Residue
B	ARG149

---

site_id	AC7
Number of Residues	4
Details	binding site for residue SO4 B 203

Chain	Residue
B	LYS2
B	TYR31
B	GLU61
B	HOH411

---

site_id	AC8
Number of Residues	5
Details	binding site for residue SO4 B 204

Chain	Residue
B	ASN9
B	ARG75
B	7MT201
B	HOH356
B	HOH369

---

site_id	AC9
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	SO4204

---

site_id	AD1
Number of Residues	2
Details	binding site for residue SO4 C 202

Chain	Residue
C	ARG149
C	HOH329

---

site_id	AD2
Number of Residues	4
Details	binding site for residue SO4 C 203

Chain	Residue
B	LYS43
C	ARG71
C	ARG75
C	HOH350

---

site_id	AD3
Number of Residues	5
Details	binding site for residue SO4 C 204

Chain	Residue
C	ASN9
C	ARG75
C	7MT201
C	HOH327
C	HOH384

---

site_id	AD4
Number of Residues	10
Details	binding site for residue 2HA C 205

Chain	Residue
A	PHE90
A	SER91
A	VAL111
A	ARG113
A	ARG115
C	ILE128
C	GLY131
C	VAL132
C	HOH347
C	HOH359

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:11114201

Chain	Residue	Details
A	CYS100
B	CYS100
C	CYS100

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00608

Chain	Residue	Details
A	HIS101
B	HIS101
C	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

---