2MAN
MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE
Summary for 2MAN
| Entry DOI | 10.2210/pdb2man/pdb |
| Descriptor | PROTEIN (BETA-MANNANASE), beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose (3 entities in total) |
| Functional Keywords | mannanase, glycosyl hydrolase, family 5, thermomonospora fusca, hydrolase |
| Biological source | Thermobifida fusca |
| Total number of polymer chains | 1 |
| Total formula weight | 33465.61 |
| Authors | Hilge, M.,Gloor, S.M.,Piontek, K. (deposition date: 1998-08-12, release date: 1999-08-13, Last modification date: 2024-11-13) |
| Primary citation | Hilge, M.,Gloor, S.M.,Rypniewski, W.,Sauer, O.,Heightman, T.D.,Zimmermann, W.,Winterhalter, K.,Piontek, K. High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5. Structure, 6:1433-1444, 1998 Cited by PubMed Abstract: . beta-Mannanases hydrolyse the O-glycosidic bonds in mannan, a hemicellulose constituent of plants. These enzymes have potential use in pulp and paper production and are of significant biotechnological interest. Thermostable beta-mannanases would be particularly useful due to their high temperature optimum and broad pH tolerance. The thermophilic actinomycete Thermomonospora fusca secretes at least one beta-mannanase (molecular mass 38 kDa) with a temperature optimum of 80 degreesC. No three-dimensional structure of a mannan-degrading enzyme has been reported until now. PubMed: 9817845DOI: 10.1016/S0969-2126(98)00142-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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