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3MAN

MANNOHEXAOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE

Summary for 3MAN
Entry DOI10.2210/pdb3man/pdb
DescriptorPROTEIN (BETA-MANNANASE), beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose (3 entities in total)
Functional Keywordsmannanase, glycosyl hydrolase, family 5, thermomonospora fusca, mannohexaose complex, hydrolase
Biological sourceThermobifida fusca
Total number of polymer chains1
Total formula weight33627.75
Authors
Hilge, M.,Gloor, S.M.,Piontek, K. (deposition date: 1998-08-12, release date: 1999-08-13, Last modification date: 2024-10-30)
Primary citationHilge, 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: 9817845
DOI: 10.1016/S0969-2126(98)00142-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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