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3W9A

Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea

Summary for 3W9A
Entry DOI10.2210/pdb3w9a/pdb
DescriptorPutative uncharacterized protein, GLYCEROL (3 entities in total)
Functional Keywordsgh131, beta-jelly roll, hydrolase
Biological sourceCoprinopsis cinerea (Inky cap fungus)
Total number of polymer chains4
Total formula weight112673.92
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 citationMiyazaki, 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: 23711369
DOI: 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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数据于2025-07-30公开中

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