wwPDB validation report of PDB entry 1H94

GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE

ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6 -PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6 -PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES COMPLEXED WITH SUBSTRATE AND NADPH

ACTIVE MUTANT (S215->C) OF GLUCOSE 6- PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+

CHAIN A ENGINEERED MUTATION SER215CYS
BETA-D-GLUCOSE 6-PHOSPHATE + NADP(+) = D-GLUCONO-DELTA-LACTONE
6-PHOSPHATE + NADPH.

BULK SOLVENT WAS MODELLED WITH DENSITY 0.311 E/A**3 AND TEMPERATURE FACTOR 31.7 A**2. THE OCCUPANCY OF COENZYME NAD HAS BEEN REDUCED TO 0.6 IN ORDER TO MATCH ITS TEMPERATURE FACTORS TO THOSE OF ATOMS IN THE NEIGHBOURING PROTEIN RESIDUES.

GLUCOSE 6-PHOSPHATE 1-DEHYDROGENASE (E.C.1.1.1.49)
COMPLEX OF ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L.MESENTEROIDES WITH COENZYME NAD

The largest off-origin peak in the Patterson function is 6.43% of the height of the origin peak. No significant pseudotranslation is detected.

structure factor analysis and validation

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

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