3W9A
Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea
Summary for 3W9A
Entry DOI | 10.2210/pdb3w9a/pdb |
Descriptor | Putative uncharacterized protein, GLYCEROL (3 entities in total) |
Functional Keywords | gh131, beta-jelly roll, hydrolase |
Biological source | Coprinopsis cinerea (Inky cap fungus) |
Total number of polymer chains | 4 |
Total formula weight | 112673.92 |
Authors | Miyazaki, T.,Tanaka, Y.,Tamura, M.,Yoshida, M.,Nishikawa, A.,Tonozuka, T. (deposition date: 2013-04-01, release date: 2013-05-22, Last modification date: 2024-10-30) |
Primary citation | Miyazaki, T.,Yoshida, M.,Tamura, M.,Tanaka, Y.,Umezawa, K.,Nishikawa, A.,Tonozuka, T. Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea Febs Lett., 587:2193-2198, 2013 Cited by PubMed Abstract: The crystal structure of the N-terminal putative catalytic domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea (CcGH131A) was determined. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B. A concave of sheet-B, the possible active site, was wide and shallow, and three glycerol molecules were present in the concave. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues, and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases. PubMed: 23711369DOI: 10.1016/j.febslet.2013.05.041 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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