4MWT

Crystal structure of human PPCA (trigonal crystal form 2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004180	molecular_function	carboxypeptidase activity
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0005576	cellular_component	extracellular region
A	0005764	cellular_component	lysosome
A	0005783	cellular_component	endoplasmic reticulum
A	0006508	biological_process	proteolysis
A	0006886	biological_process	intracellular protein transport
A	0008047	molecular_function	enzyme activator activity
A	0008233	molecular_function	peptidase activity
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0031647	biological_process	regulation of protein stability
A	0035578	cellular_component	azurophil granule lumen
A	0043202	cellular_component	lysosomal lumen
A	0070062	cellular_component	extracellular exosome
A	0098575	cellular_component	lumenal side of lysosomal membrane
A	1904714	biological_process	regulation of chaperone-mediated autophagy
A	1904715	biological_process	negative regulation of chaperone-mediated autophagy
B	0004180	molecular_function	carboxypeptidase activity
B	0004185	molecular_function	serine-type carboxypeptidase activity
B	0005576	cellular_component	extracellular region
B	0005764	cellular_component	lysosome
B	0005783	cellular_component	endoplasmic reticulum
B	0006508	biological_process	proteolysis
B	0006886	biological_process	intracellular protein transport
B	0008047	molecular_function	enzyme activator activity
B	0008233	molecular_function	peptidase activity
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0031647	biological_process	regulation of protein stability
B	0035578	cellular_component	azurophil granule lumen
B	0043202	cellular_component	lysosomal lumen
B	0070062	cellular_component	extracellular exosome
B	0098575	cellular_component	lumenal side of lysosomal membrane
B	1904714	biological_process	regulation of chaperone-mediated autophagy
B	1904715	biological_process	negative regulation of chaperone-mediated autophagy

Functional Information from PROSITE/UniProt

site_id	PS00131
Number of Residues	8
Details	CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. LtGESYAG

Chain	Residue	Details
A	LEU146-GLY153

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site_id	PS00560
Number of Residues	18
Details	CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. IafLtIkGAGHmVPtdkP

Chain	Residue	Details
A	ILE419-PRO436

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
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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