1uwc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
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.
+
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.
==About this Structure==
==About this Structure==
Line 14: Line 14:
[[Category: Feruloyl esterase]]
[[Category: Feruloyl esterase]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Mcauley, K.E.]]
+
[[Category: Mcauley, K E.]]
-
[[Category: Patkar, S.A.]]
+
[[Category: Patkar, S A.]]
[[Category: Svendsen, A.]]
[[Category: Svendsen, A.]]
-
[[Category: Wilson, K.S.]]
+
[[Category: Wilson, K S.]]
[[Category: FER]]
[[Category: FER]]
[[Category: NAG]]
[[Category: NAG]]
Line 25: Line 25:
[[Category: xylan degradation]]
[[Category: xylan degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:08:38 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:01 2008''

Revision as of 13:29, 21 February 2008


1uwc, resolution 1.08Å

Drag the structure with the mouse to rotate

FERULOYL ESTERASE FROM ASPERGILLUS NIGER

Overview

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.

About this Structure

1UWC is a Single protein structure of sequence from Aspergillus niger with , and as ligands. Active as Feruloyl esterase, with EC number 3.1.1.73 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 15:29:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools