4NOJ: VAST+ Similar Structure Assemblies and Proteins

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Biotechnology Information

Crystal structure of the mature form of asparaginyl endopeptidase (AEP)/Legumain activated at pH 3.5

Biological unit 1:	monomeric
Source organism:	Mus musculus
Number of proteins:	1 (Legumain)

Similar Structures (478)

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			PDB ID	Description	Taxonomy▲▼	Aligned Protein▲▼	RMSD▲▼	Aligned Residues▲▼	Sequence Identity▲▼
1	Expand row	Full	4AWA	Crystal structure of active legumain in complex with YVAD-CMK at pH 5.0	Others	1	0.40Å	260	91%
2	Expand row	Full	4NOM	Crystal Structure Of Asparaginyl Endopeptidase (aep)/legumain Activated At Ph 4.5	Mus musculus	1	0.41Å	260	100%
3	Expand row	Full	4NOK	Crystal Structure Of Proenzyme Asparaginyl Endopeptidase (aep) /legumain At Ph 7.5	Mus musculus	1	0.41Å	260	100%
4	Expand row	Full	4AW9	Crystal Structure Of Active Legumain In Complex With Yvad-cmk	Others	1	0.41Å	260	91%
5	Expand row	Full	4NOL	Crystal Structure Of Proenzyme Asparaginyl Endopeptidase (aep) /legumain Mutant D233a At Ph 7.5	Mus musculus	1	0.42Å	260	99%
6	Expand row	Full	4AWB	Crystal structure of active legumain in complex with AAN-CMK	Homo sapiens	1	0.43Å	260	91%
7	Expand row	Full	4FGU	Crystal Structure Of Prolegumain	Homo sapiens	1	0.67Å	260	91%
8	Expand row	Full	5LU8	CRYSTAL STRUCTURE OF YVAD-CMK BOUND HUMAN LEGUMAIN (AEP) IN COMPLEX WITH COMPOUND 11B	Others	1	0.38Å	259	91%
9	Expand row	Full	4D3X	The structure of mature legumain from chinese hamster	Cricetulus griseus	1	0.38Å	259	95%
10	Expand row	Full	5LU9	Crystal structure of YVAD-cmk bound human legumain (AEP) in complex with compound 11	Others	1	0.38Å	259	91%

{"1":"Legumain"}

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?Original VAST

Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.