1X38
crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole
Summary for 1X38
Entry DOI | 10.2210/pdb1x38/pdb |
Related | 1LQ2 1X39 |
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 | 68292.09 |
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 Cited by PubMed: 16342944DOI: 10.1021/bi0514818 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.698 Å) |
Structure validation
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