8B57

Structure of prolyl endoprotease from Aspergillus niger CBS 109712

Summary for 8B57

• Entry DOI: 10.2210/pdb8b57/pdb
• Descriptor: Prolyl Endoprotease from Aspergillus niger CBS 109712, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• Functional Keywords: endoprotease, proline-specific, s28 peptidase, hydrolase
• Biological source: Aspergillus niger
• Total number of polymer chains: 1
• Total formula weight: 58797.44

Authors

Pijning, T.,Vujicic-Zagar, A.,Van der Laan, J.M.,De Jong, R.M.,Dijkstra, B.W. (deposition date: 2022-09-22, release date: 2023-12-20, Last modification date: 2024-01-10)

• Primary citation: Pijning, T.,Vujicic-Zagar, A.,van der Laan, J.M.,de Jong, R.M.,Ramirez-Palacios, C.,Vente, A.,Edens, L.,Dijkstra, B.W.; Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.; Protein Sci., 33:e4856-e4856, 2024; PubMed: 38059672; DOI: 10.1002/pro.4856

Experimental method

X-RAY DIFFRACTION (2.42 Å)