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Structure paper

TitleMechanistic and Structural Studies on Legumain Explain its Zymogenicity, Distinct Activation Pathways, and Regulation
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 110, Page 10940-, Year 2013
Publish dateJun 1, 2012 (structure data deposition date)
AuthorsDall, E. / Brandstetter, H.
External linksProc. Natl. Acad. Sci. USA / PubMed:23776206
MethodsX-ray diffraction
Resolution2.2 - 3.9 Å
Structure data

PDB-4aw9:
Crystal structure of active legumain in complex with YVAD-CMK
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4awa:
Crystal structure of active legumain in complex with YVAD-CMK at pH 5.0
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4awb:
Crystal structure of active legumain in complex with AAN-CMK
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4fgu:
Crystal structure of prolegumain
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-HG:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / CYSTEINE PROTEASE / LYSOSOMAL / AEP / SUBSTRATE SPECIFICITY / MHCII / ANTIGEN PROCESSING / CANCER / HYDROLASE/INHIBITOR / HYDROLASE-INHIBITOR COMPLEX / HYDROLASE / ASPARAGINYL ENDOPEPTIDASE / PROENZYME

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