wwPDB validation report of PDB entry 2CKS

ENDOGLUCANASE CEL5A, ENDO-1,4-BETA-GLUCANASE E-4, CELLULASE E-5, CELLULASE E5

X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THERMOBIFIDA FUSCA ENDOGLUCANASE CEL5A (E5) E355Q IN COMPLEX WITH CELLOTETRAOSE

ENDOHYDROLYSIS OF 1,4-BETA-D-GLUCOSIDIC LINKAGES IN CELLULOSE, LICHENIN AND CEREAL BETA-D-GLUCANS

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FOLLOWING RESIDUES HAVE BEEN MODELLED IN MULTIPLE CONFORMATIONS A136, A138, A143, A166, A169, A206, A207, A248, A263, A271, A274, A289, A290, A305, A323, A337, A343, A378, A388, A416, A425, A1431, B131, B138, B143, B166, B169, B206, B225, B248, B249, B252, B263, B271, B274, B289, B290, B297, B321, B343, B422, B1431, Y46, Y69, Y71, Y82, Y128, Y172, Y215, Y221, Y260, Y267, Z137, Z187, Z246, Z256, Z273, Z277, Z279, Z284, Z289. ATOMS WITH MISSING ELECTRON DENSITY ARE ASSIGNED ZERO OCCUPANCY. ATOMS ARE ASSIGNED REDUCED OCCUPANCIES WHEN ELECTRON DENSITY IS WEAK OR ATOMS HAVE PARTIAL OCCUPANCY. NO NCS CONSTRAINTS OR RESTRAINTS HAVE BEEN USED IN REFINEMENT OF THE TWO PROTEIN CHAINS IN THE ASYMMETRIC UNIT.
THEORETICAL MODEL PRODUCED BY SWISS-MODEL

X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THERMOBIFIDA FUSCA ENDOGLUCANASE CEL5A (E5)

The largest off-origin peak in the Patterson function is 5.81% 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