1AUG

CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0016920	molecular_function	pyroglutamyl-peptidase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008234	molecular_function	cysteine-type peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0016920	molecular_function	pyroglutamyl-peptidase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008234	molecular_function	cysteine-type peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0016920	molecular_function	pyroglutamyl-peptidase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008234	molecular_function	cysteine-type peptidase activity
D	0016787	molecular_function	hydrolase activity
D	0016920	molecular_function	pyroglutamyl-peptidase activity

Functional Information from PROSITE/UniProt

site_id	PS01333
Number of Residues	17
Details	PYRASE_GLU Pyrrolidone-carboxylate peptidase glutamic acid active site. GqaGgrmqITpERVAiN

Chain	Residue	Details
A	GLY70-ASN86

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site_id	PS01334
Number of Residues	15
Details	PYRASE_CYS Pyrrolidone-carboxylate peptidase cysteine active site. IpAaVSyTAGtFVCN

Chain	Residue	Details
A	ILE131-ASN145

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 10196127, 8095933, 8655512

Chain	Residue	Details
A	GLU81
A	CYS144
A	CYS144
A	ARG91
A	HIS168

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site_id	CSA2
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 10196127, 8095933, 8655512

Chain	Residue	Details
B	GLU291
B	CYS354
B	CYS354
B	HIS378
B	ARG301

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site_id	CSA3
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 10196127, 8095933, 8655512

Chain	Residue	Details
C	HIS588
C	CYS564
C	CYS564
C	ARG511
C	GLU501

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site_id	CSA4
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 10196127, 8095933, 8655512

Chain	Residue	Details
D	HIS798
D	CYS774
D	CYS774
D	ARG721
D	GLU711

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 633

Chain	Residue	Details
A	GLU81	electrostatic stabiliser
A	ARG91	electrostatic stabiliser
A	CYS144	electrostatic stabiliser
A	HIS168	proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 633

Chain	Residue	Details
B	GLU291	electrostatic stabiliser
B	ARG301	electrostatic stabiliser
B	CYS354	electrostatic stabiliser
B	HIS378	proton acceptor, proton donor

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site_id	MCSA3
Number of Residues	4
Details	M-CSA 633

Chain	Residue	Details
C	GLU501	electrostatic stabiliser
C	ARG511	electrostatic stabiliser
C	CYS564	electrostatic stabiliser
C	HIS588	proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	4
Details	M-CSA 633

Chain	Residue	Details
D	GLU711	electrostatic stabiliser
D	ARG721	electrostatic stabiliser
D	CYS774	electrostatic stabiliser
D	HIS798	proton acceptor, proton donor

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