1RMG
RHAMNOGALACTURONASE A FROM ASPERGILLUS ACULEATUS
Summary for 1RMG
| Entry DOI | 10.2210/pdb1rmg/pdb |
| Descriptor | RHAMNOGALACTURONASE A, alpha-D-mannopyranose-(1-3)-[beta-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, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | hydrolase, inverting, parallel beta-helix, glycosidase |
| Biological source | Aspergillus aculeatus |
| Total number of polymer chains | 1 |
| Total formula weight | 48929.94 |
| Authors | Petersen, T.N.,Kauppinen, S.,Larsen, S. (deposition date: 1997-02-26, release date: 1998-03-04, Last modification date: 2024-10-09) |
| Primary citation | Petersen, T.N.,Kauppinen, S.,Larsen, S. The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix. Structure, 5:533-544, 1997 Cited by PubMed Abstract: Pectic substances are the major polysaccharide components of the middle lamella and primary cell wall of dicotyledonous plants. They consist of homogalacturonan 'smooth' regions and highly rhamnified 'hairy' regions of rhamnogalacturonan. The backbone in rhamnogalacturonan-l (RG-l), which is composed of alternating galacturonic acid and rhamnose residues, is the substrate for a new class of enzymes known as rhamnogalacturnoases (RGases). RGase A is a novel enzyme implicated in the enzymatic degradation of RG-l. PubMed: 9115442DOI: 10.1016/S0969-2126(97)00209-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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