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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
B0004866molecular_functionendopeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005773cellular_componentvacuole
B0019828molecular_functionaspartic-type endopeptidase 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: Reactive bond for trypsin
ChainResidueDetails
AARG67
BARG67

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Reactive bond for chymotrypsin => ECO:0000250
ChainResidueDetails
AMET111
BMET111

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:26542926, ECO:0000269|PubMed:2753167, ECO:0007744|PDB:5DZU
ChainResidueDetails
AASN19
BASN19

222624

PDB entries from 2024-07-17

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