Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with 4-O-methyl glucuronic acid

4-O-methyl-alpha-D-glucopyranuronic acid

The Mechanisms by which Family 10 Glycoside Hydrolases Bind Decorated Substrates

ENGINEERED MUTATION GLU 262 SER IN COORDS

4-O-methyl-alpha-D-glucopyranuronic acid-(1-2)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose

STRUCTURE ISOMORPHOUS WITH STARTING MODEL

0.1M MGCL2 0.1M TRIS HCL PH6.5, 30% PEG 4K, 5% ISOPROPANOL, pH 6.50

XYLANASE XYN10B MUTANT (E262S) FROM CELLVIBRIO MIXTUS IN COMPLEX WITH XYLOPENTAOSE

XYLANASE XYN10B MUTANT (E262S) FROM CELLVIBRIO MIXTUS IN COMPLEX WITH ARABINOFURANOSE ALPHA -1,3 LINKED TO XYLOBIOSE

XYLANASE XYN10B MUTANT (E262S) FROM CELLVIBRIO MIXTUS IN COMPLEX WITH ARABINOFURANOSE ALPHA 1,3 LINKED TO XYLOTRIOSE

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

ENGINEERED MUTATION GLU 271 SER IN THE SWISSPROT DATABASE REFERENCE

THE SEQUENCE ON THE DATABASE IS INCORRECT AND WILL
BE CHANGED BY THE AUTHORS.
THESE DISCREPANCIES ARE F36L, N37I, R38G, R39A,
R40A, K216E, T221R, R222G, Y271V, E290D, R291P, M342I.
THE SEQUENCE WAS EXPRESSED IN PET21A.
THIS ACCOUNTS FOR THE A1M SUBSTITION AND THE ADDITION
OF HIS TAG RESIDUES 271-278.
THE FIRST 9 RESIDUES IN THE DATABASE HAVE BEEN OMITTED.
E262S IS AN ENGINEERED MUTATION.

THIS ENTRY HAS ATOMS REFINED WITH AN OCCUPANCY OF 0.00

HYDROLASE, FAMILY 10, XYLANASE, GLYCOSIDE HYDROLASE, HEMICELLULOSE, XYLAN DEGRADATION