1AZW

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016787	molecular_function	hydrolase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AS
Number of Residues	3
Details	ACTIVE-SITE.

Chain	Residue
A	GLY100
A	ASP266
A	HIS294

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:9427736

Chain	Residue	Details
A	SER110
B	SER110

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:9427736

Chain	Residue	Details
A	ASP266
B	ASP266

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:9427736

Chain	Residue	Details
A	HIS294
B	HIS294

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 412

Chain	Residue	Details
A	GLY43	electrostatic stabiliser
A	SER110	covalent catalysis, proton shuttle (general acid/base)
A	TRP111	electrostatic stabiliser
A	ASP266	electrostatic stabiliser
A	HIS294	electrostatic stabiliser, proton shuttle (general acid/base)

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 412

Chain	Residue	Details
B	GLY43	electrostatic stabiliser
B	SER110	covalent catalysis, proton shuttle (general acid/base)
B	TRP111	electrostatic stabiliser
B	ASP266	electrostatic stabiliser
B	HIS294	electrostatic stabiliser, proton shuttle (general acid/base)

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