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5DZU

Structure of potato cathepsin D inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005773cellular_componentvacuole
A0019828molecular_functionaspartic-type endopeptidase inhibitor activity
A0030414molecular_functionpeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005773cellular_componentvacuole
B0019828molecular_functionaspartic-type endopeptidase inhibitor activity
B0030414molecular_functionpeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. LlETGGTIG
ChainResidueDetails
ALEU112-GLY120

site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. VlDTNGKeLnPNssYrI
ChainResidueDetails
AVAL8-ILE24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSite: {"description":"Reactive bond for trypsin"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Reactive bond for chymotrypsin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26542926","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2753167","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DZU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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