wwPDB validation report of PDB entry 1PJS

RESIDUES 1-212 (CYSGB) ARE A DEHYDROGENASE/FERROCHELATASE, RESIDUES 213-457 (CYSGA) ARE A BISMETHYLTRANSFERASE

The co-crystal structure of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis, in complex with it NAD cofactor

The asymmetric unit contains a single homodimer.
Each of CysG's modules (CysGB, residues 1-212, and CysGA, residues 213-457)
are homodimers. Each subunit contains half of CysGB and half of CysGA, each of which is related
to its dimer partner by
a unique non-crystallographic two-fold symmetry axis.
CysG has two distinct non-crystallographic two-fold
symmetry axes, one for each homodimeric module.

The largest off-origin peak in the Patterson function is 6.59% 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)