wwPDB validation report of PDB entry 1O00

Complete mature sequence (does not contain mitochondrial leader sequence).

Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mn2+

Aldehyde dehydrogenase from bovine mitochondria (Apo)

Aldehyde dehydrogenase from bovine mitochondria complexed with NAD and Sm3+

Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NADH and Mg2+

Human mitochondrial aldehyde dehydrogenase complexed with NAD+ in the presence of low Mg2+

Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of low Mg2+

Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(H) and Mg2+

Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of Mg2+

Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+

Apo form of human mitochondrial aldehyde dehydrogenase

maximum likelihood target using amplitudesmaximum likelihood target using amplitudes
Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ showing dual NAD(H) conformations
The analyses of the Patterson function reveals a significant off-origin peak that is 58.80 % of the origin peak, indicating pseudo-translational symmetry. The chance of finding a peak of this or larger height by random in a structure without pseudo-translational symmetry is equal to 1.9385e-05. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.
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)