1DEU

CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN X: A CYSTEINE PROTEASE WITH THE PROREGION COVALENTLY LINKED TO THE ACTIVE SITE CYSTEINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002003	biological_process	angiotensin maturation
A	0004180	molecular_function	carboxypeptidase activity
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005764	cellular_component	lysosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005886	cellular_component	plasma membrane
A	0005938	cellular_component	cell cortex
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0009986	cellular_component	cell surface
A	0010757	biological_process	negative regulation of plasminogen activation
A	0016787	molecular_function	hydrolase activity
A	0016807	molecular_function	cysteine-type carboxypeptidase activity
A	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
A	0030426	cellular_component	growth cone
A	0031012	cellular_component	extracellular matrix
A	0031410	cellular_component	cytoplasmic vesicle
A	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
A	0035580	cellular_component	specific granule lumen
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0060441	biological_process	epithelial tube branching involved in lung morphogenesis
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0002003	biological_process	angiotensin maturation
B	0004180	molecular_function	carboxypeptidase activity
B	0004197	molecular_function	cysteine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005764	cellular_component	lysosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005886	cellular_component	plasma membrane
B	0005938	cellular_component	cell cortex
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008234	molecular_function	cysteine-type peptidase activity
B	0009986	cellular_component	cell surface
B	0010757	biological_process	negative regulation of plasminogen activation
B	0016787	molecular_function	hydrolase activity
B	0016807	molecular_function	cysteine-type carboxypeptidase activity
B	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
B	0030426	cellular_component	growth cone
B	0031012	cellular_component	extracellular matrix
B	0031410	cellular_component	cytoplasmic vesicle
B	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
B	0035580	cellular_component	specific granule lumen
B	0051603	biological_process	proteolysis involved in protein catabolic process
B	0060441	biological_process	epithelial tube branching involved in lung morphogenesis
B	0070062	cellular_component	extracellular exosome
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00640
Number of Residues	20
Details	THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgepWGerGWLrI

Chain	Residue	Details
A	TYR195-ILE214

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"10656802","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10745011","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
A	CYS31
A	ASN200
A	HIS180

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
B	CYS31
B	ASN200
B	HIS180

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
A	GLN22
A	CYS31
A	HIS180

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
B	GLN22
B	CYS31
B	HIS180

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
A	GLN22
A	ASN200
A	HIS180

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1pad

Chain	Residue	Details
B	GLN22
B	ASN200
B	HIS180

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 953

Chain	Residue	Details
A	GLN22	electrostatic stabiliser
A	CYS31	covalent catalysis, proton shuttle (general acid/base)
A	HIS180	proton shuttle (general acid/base)
A	ASN200	electrostatic stabiliser, modifies pKa

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 953

Chain	Residue	Details
B	GLN22	electrostatic stabiliser
B	CYS31	covalent catalysis, proton shuttle (general acid/base)
B	HIS180	proton shuttle (general acid/base)
B	ASN200	electrostatic stabiliser, modifies pKa

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