wwPDB validation report of PDB entry 2VIG

SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE,

SCAD, BUTYRYL-COA DEHYDROGENASE, ACYL COA DEHYDROGENASE

GLY209 -> SER CHANGE IS A NATURAL VARIANT

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DENSITY ADJACENT TO FAD IN THE ACTIVE SITE HAS BEEN MODELLED AS COENZYME-A PERSULPHIDE. BOUND COS IS MOST APPARENT IN CHAIN G BUT NOT FULLY OCCUPIED IN OTHER CHAINS. NO ATTEMPT WAS MADE TO MODEL OCCUPANCY SO TEMPERATURE FACTORS ARE HIGH.
SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, (E.C.1.3.99.2)
Crystal structure of human short-chain acyl CoA dehydrogenase
The largest off-origin peak in the Patterson function is 2.70% 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)