1uwc | pdb_00001uwc
From Proteopedia
FERULOYL ESTERASE FROM ASPERGILLUS NIGER
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Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site. Structure of a feruloyl esterase from Aspergillus niger.,McAuley KE, Svendsen A, Patkar SA, Wilson KS Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 21:54, 28 September 2014.