wwPDB validation report of PDB entry 5FHM

Protein crystallized is the extracellular ligand-binding domain of GluA2. Transmembrane regions genetically removed and replaced with Gly-Thr linker (residues 118-119). Protein consists of UNP residues 413-527 and 653-797, numbering with signal peptide of 21 residues. The first two residues (Gly, Ala) are cloning remnants.
Glutamate receptor 2,Glutamate receptor 2

(2~{S})-3-[5-[2-[[3-(aminomethyl)phenyl]methyl]-1,2,3,4-tetrazol-5-yl]-3-oxidanyl-1,2-oxazol-4-yl]-2-azanyl-propanoic acid

GluR-2,AMPA-selective glutamate receptor 2,GluR-B,GluR-K2,Glutamate receptor ionotropic,AMPA 2,GluA2,Ionotropic glutamate receptor A2,GluR-2,AMPA-selective glutamate receptor 2,GluR-B,GluR-K2,Glutamate receptor ionotropic,AMPA 2,GluA2,Ionotropic glutamate receptor A2

2P2A contains the same protein in omplex with a related ligand

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with (S)-2-Amino-3-(5-(2-(3-(aminomethyl)benzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid at resolution 1.55 A resolution

The largest off-origin peak in the Patterson function is 8.69% 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)