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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
B0008544biological_processepidermis development
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
DetailsSITE: Reactive site
ChainResidueDetails
BGLY11

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN112

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23776206
ChainResidueDetails
AASN91
AASN167

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23776206
ChainResidueDetails
AGLN263
AASN272

221051

PDB entries from 2024-06-12

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