1UWC
Feruloyl esterase from Aspergillus niger
Summary for 1UWC
Entry DOI | 10.2210/pdb1uwc/pdb |
Related | 1USW |
Descriptor | FERULOYL ESTERASE A, 2-acetamido-2-deoxy-beta-D-glucopyranose, 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID, ... (5 entities in total) |
Functional Keywords | hydrolase, serine esterase, xylan degradation |
Biological source | ASPERGILLUS NIGER |
Total number of polymer chains | 2 |
Total formula weight | 58161.19 |
Authors | McAuley, K.E.,Svendsen, A.,Patkar, S.A.,Wilson, K.S. (deposition date: 2004-02-03, release date: 2004-05-06, Last modification date: 2024-11-13) |
Primary citation | Mcauley, K.E.,Svendsen, A.,Patkar, S.A.,Wilson, K.S. Structure of a Feruloyl Esterase from Aspergillus Niger Acta Crystallogr.,Sect.D, 60:878-, 2004 Cited by PubMed Abstract: The 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. PubMed: 15103133DOI: 10.1107/S0907444904004937 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.08 Å) |
Structure validation
Download full validation report