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5ZBI

Crystal structure of asparaginyl endopeptidases from Viola Canadensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005773cellular_componentvacuole
A0006508biological_processproteolysis
A0006624biological_processvacuolar protein processing
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0051603biological_processproteolysis involved in protein catabolic process
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005773cellular_componentvacuole
B0006508biological_processproteolysis
B0006624biological_processvacuolar protein processing
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 501
ChainResidue
AHIS374
ASER430
ALEU431
ASER432
AGLU433
ATYR434

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
ALYS-30-ASP-5

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PDB entries from 2024-05-01

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