1X39

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole

Summary for 1X39

• Entry DOI: 10.2210/pdb1x39/pdb
• Related: 1LQ2 1X38
• Descriptor: beta-D-glucan exohydrolase isoenzyme ExoI, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[beta-D-xylopyranose-(1-2)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: 2-domain fold, ligand-protein complex, hydrolase
• Biological source: Hordeum vulgare
• Total number of polymer chains: 1
• Total formula weight: 68509.29

Authors

Hrmova, M.,Streltsov, V.A.,Smith, B.J.,Vasella, A.,Varghese, J.N.,Fincher, G.B. (deposition date: 2005-05-02, release date: 2005-12-20, Last modification date: 2023-10-25)

• Primary citation: Hrmova, M.,Streltsov, V.A.,Smith, B.J.,Vasella, A.,Varghese, J.N.,Fincher, G.B.; Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley.; Biochemistry, 44:16529-16539, 2005; PubMed: 16342944; DOI: 10.1021/bi0514818

Experimental method

X-RAY DIFFRACTION (1.8 Å)