wwPDB validation report of PDB entry 4IZ6

Enterobactin synthase component E, Isochorismatase
Fusion between EntE(1-536) and EntB(211-285)

Enterochelin synthase E, 2,3-dihydroxybenzoate-AMP ligase, Dihydroxybenzoic acid-activating enzyme, S-dihydroxybenzoyltransferase, 3 dihydro-2, 3 dihydroxybenzoate synthase, Enterobactin synthase component B, Enterochelin synthase B, Isochorismate lyase

THE 1HZ LIGAND IS ATTACHED TO PHOSPHOPANTETHEINE (PNS) THIOL (S44) TO FORM A COVALENT LINKAGE. THE LIGAND 1HZ REPRESENTS THE FINAL BOUND PRODUCT. THE STARTING MATERIAL FOR 1HZ LIGAND ((E)-5'-AMINO-5'-DEOXY-5'-N-{[2-(2,3-HYDROXYPHENYL)ETHENYL]SULFONYL}ADENOSINE) HAS A DOUBLE BOND BETWEEN C21 AND C22 ATOM GROUPS.
THE STRUCTURE IS A CHIMERIC PROTEIN OF ENTEROBACTIN SYNTHETASE COMPONENT E (ENTE) AND THE CARRIER PROTEIN DOMAIN OF 2,3-DIHYDRO-2,3-DIHYDROXYBENZOATE SYNTHETASE, ISOCHROISMATASE (ENTB) JOINED BY GLY-ARG-ALA-SER LINKER RESIDUES BETWEEN THESE TWO PROTEINS.

Enterobactin synthase component E, Isochorismatase (E.C.2.7.7.58, 2.3.1.-)
Structure of EntE and EntB, an NRPS adenylation-PCP fusion protein with pseudo translational symmetry

The analyses of the Patterson function reveals a significant off-origin peak that is 59.58 % 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 1.7283e-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)