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7O50

Crystal structure of human legumain in complex with Gly-Ser-Asn peptide

Summary for 7O50
Entry DOI10.2210/pdb7o50/pdb
DescriptorLegumain, GLY-SER-ASN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsenzyme, cysteine protease, ligase, asparaginyl endopeptidase, substrate, hydrolase
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight62209.35
Authors
Dall, E.,Brandstetter, H. (deposition date: 2021-04-07, release date: 2021-09-22, Last modification date: 2024-01-31)
Primary citationDall, E.,Stanojlovic, V.,Demir, F.,Briza, P.,Dahms, S.O.,Huesgen, P.F.,Cabrele, C.,Brandstetter, H.
The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities.
Acs Catalysis, 11:11885-11896, 2021
Cited by
PubMed: 34621593
DOI: 10.1021/acscatal.1c02057
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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