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4NOK

Crystal structure of proenzyme asparaginyl endopeptidase (AEP)/Legumain at pH 7.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0051603biological_processproteolysis involved in protein catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9891971
ChainResidueDetails
AHIS150

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9891971
ChainResidueDetails
ACYS191

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by autolysis
ChainResidueDetails
AASN325

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN93
AASN169
AASN265
AASN274

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PDB entries from 2024-05-08

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