wwPDB validation report of PDB entry 2IVQ

CYANASE LYASE, CYANASE, CYANATE HYDROLASE

STRUCTURE OF CYANASE REVEALS THAT A NOVEL DIMERIC AND DECAMERICARRANGEMENT OF SUBUNITS IS REQUIRED FOR FORMATION OF THE ENZYME ACTIVESITE

STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE

SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE

CATALYZES THE REACTION OF CYANATE WITH BICARBONATE TO
PRODUCE AMMONIA AND CARBON DIOXIDE.

ENGINEERED RESIDUE IN CHAIN A, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN B, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN C, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN D, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN E, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN F, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN G, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN H, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN I, ARG 96 TO LYS
ENGINEERED RESIDUE IN CHAIN J, ARG 96 TO LYS

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

geometric validation package for ligand chemistry in protein x-ray structures
20191225.v01 (using entries in the PDB archive December 25th 2019)