1L1Y

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

Summary for 1L1Y

• Entry DOI: 10.2210/pdb1l1y/pdb
• Related: 1L2A
• Related PRD ID: PRD_900005
• Descriptor: cellobiohydrolase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (3 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: 461883.70

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 (2.4 Å)