6Q3R
ASPERGILLUS ACULEATUS GALACTANASE
Summary for 6Q3R
Entry DOI | 10.2210/pdb6q3r/pdb |
Related PRD ID | PRD_900113 |
Descriptor | Arabinogalactan endo-beta-1,4-galactanase, TRIETHYLENE GLYCOL, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total) |
Functional Keywords | aspergillus aculeatus galactanase complex with galactobiose, hydrolase |
Biological source | Aspergillus aculeatus |
Total number of polymer chains | 2 |
Total formula weight | 77902.55 |
Authors | Muderspach, S.J.,Torpenholt, S.,Lo Leggio, L.,Poulsen, J.C.N. (deposition date: 2018-12-04, release date: 2019-06-12, Last modification date: 2024-11-06) |
Primary citation | Torpenholt, S.,Poulsen, J.C.N.,Muderspach, S.J.,De Maria, L.,Lo Leggio, L. Structure of Aspergillus aculeatus beta-1,4-galactanase in complex with galactobiose. Acta Crystallogr.,Sect.F, 75:399-404, 2019 Cited by PubMed Abstract: β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases. PubMed: 31204685DOI: 10.1107/S2053230X19005612 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
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