1LYB

CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIVDTGTSLMVG

Chain	Residue	Details
B	ALA228-GLY239
A	VAL30-VAL41

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:8393577

Chain	Residue	Details
B	ASP231
D	ASP231

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8393577

Chain	Residue	Details
B	ASN199
D	ASN199

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
A	ASP33
B	ASP231

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
C	ASP33
D	ASP231

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