1L2A

The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome

Summary for 1L2A

• Entry DOI: 10.2210/pdb1l2a/pdb
• Related: 1L1Y
• Related PRD ID: PRD_900005 PRD_900020
• Descriptor: cellobiohydrolase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: alpha/alpha barrel, hydrolase
• Biological source: Clostridium thermocellum
• Cellular location: Secreted: P38686
• Total number of polymer chains: 6
• Total formula weight: 467828.86

Authors

Guimaraes, B.G.,Souchon, H.,Lytle, B.L.,Wu, J.H.D.,Alzari, P.M. (deposition date: 2002-02-20, release date: 2002-07-17, Last modification date: 2024-02-14)

• Primary citation: Guimaraes, B.G.,Souchon, H.,Lytle, B.L.,David Wu, J.H.,Alzari, P.M.; The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome.; J.Mol.Biol., 320:587-596, 2002; PubMed: 12096911; DOI: 10.1016/S0022-2836(02)00497-7

Experimental method

X-RAY DIFFRACTION (2.5 Å)