7O50
Crystal structure of human legumain in complex with Gly-Ser-Asn peptide
Summary for 7O50
Entry DOI | 10.2210/pdb7o50/pdb |
Descriptor | Legumain, GLY-SER-ASN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | enzyme, cysteine protease, ligase, asparaginyl endopeptidase, substrate, hydrolase |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 62209.35 |
Authors | Dall, E.,Brandstetter, H. (deposition date: 2021-04-07, release date: 2021-09-22, Last modification date: 2024-01-31) |
Primary citation | Dall, 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: 34621593DOI: 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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