wwPDB validation report of PDB entry 1V0N

XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A

XYLANASE 10A FROM SREPTOMYCES LIVIDANS. CELLOBIOSYL-ENZYME INTERMEDIATE AT 1.7 A

XYLANASE 10A FROM SREPTOMYCES LIVIDANS. NATIVE STRUCTURE AT 1.2 ANGSTROM RESOLUTION

XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME INTERMEDIATE AT 1.65 A

STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13

STREPTOMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13 IN COMPLEXWITH LACTOSE

STREPROMYCES LIVIDANS XYLAN BINDING DOMAIN CBM13 IN COMPLEXWITH XYLOPENTAOSE

XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-ISOFAGOMINE LACTAM

XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-ISOFAGOMINE AT PH 5.8

XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-DEOXYNOJIRIMYCIN AT PH 5.8

XYLANASE XYN10A FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH XYLOBIO-DEOXYNOJIRIMYCIN AT PH 7.5

CONTRIBUTES TO THE HYDROLYSIS OF HEMICELLULOSE, WHICH IS THE MAJOR COMPONENT OF PLANT CELL-WALLS. XLNA AND XLNB SEEM TO ACT SEQUENTIALLY ON THE SUBSTRATE TO YIELD XYLOBIOSE AND XYLOSE AS CARBON SOURCES.
THE FIRST 41 RESIDUES IN THE DATABASE CORRESPOND TO THE SIGNAL PEPTIDE. THE NUMBERING USED IN THE PDB FILE IF AFTER CLEAVAGE OF THE SIGNAL PEPTIDE.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Xylanase Xyn10a from Streptomyces lividans in complex with xylobio-isofagomine at pH 7.5

The largest off-origin peak in the Patterson function is 6.85% of the height of the origin peak. No significant pseudotranslation is detected.

20191225.v01 (using entries in the PDB archive December 25th 2019)

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures