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 Cited by PubMed: 12096911DOI: 10.1016/S0022-2836(02)00497-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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