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4N6O

Crystal structure of reduced legumain in complex with cystatin E/M

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
B0001533cellular_componentcornified envelope
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0009653biological_processanatomical structure morphogenesis
B0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00287
Number of Residues14
DetailsCYSTATIN Cysteine proteases inhibitors signature. SQLVAGIKYfLTME
ChainResidueDetails
BSER54-GLU67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"23776206","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23776206","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23776206","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23776206","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsMotif: {"description":"Secondary area of contact"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Reactive site"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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