Zinc in PDB 8rqa: Crystal Structure of Crbn-Midi in Complex with Lenalidomide

The structure of Crystal Structure of Crbn-Midi in Complex with Lenalidomide, PDB code: 8rqa was solved by Z.J.Rutter, A.Kroupova, D.Zollman, A.Ciulli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.54 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	51.989, 95.717, 148.252, 90, 90, 90
R / Rfree (%)	30 / 34.2

The binding sites of Zinc atom in the Crystal Structure of Crbn-Midi in Complex with Lenalidomide (pdb code 8rqa). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Crbn-Midi in Complex with Lenalidomide, PDB code: 8rqa:

Zinc binding site 1 out of 1 in the Crystal Structure of Crbn-Midi in Complex with Lenalidomide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Crbn-Midi in Complex with Lenalidomide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:94.7 occ:1.00 SG A:CYS323 2.4 93.8 1.0 SG A:CYS326 2.4 87.8 1.0 SG A:CYS391 2.4 71.7 1.0 OE1 A:GLN325 2.9 88.8 1.0 SG A:CYS394 3.0 106.1 1.0 CB A:CYS326 3.6 93.9 1.0 N A:CYS394 3.6 99.8 1.0 CB A:CYS394 3.6 96.5 1.0 CB A:CYS391 3.6 77.8 1.0 CB A:CYS323 3.7 86.4 1.0 CB A:ILE393 3.8 104.1 1.0 N A:CYS326 3.9 97.5 1.0 CD A:GLN325 4.0 84.9 1.0 CA A:CYS394 4.2 99.0 1.0 CA A:CYS326 4.4 97.1 1.0 C A:ILE393 4.4 101.2 1.0 CA A:ILE393 4.5 97.5 1.0 CB A:GLN325 4.6 90.7 1.0 OG1 A:THR329 4.6 84.2 1.0 N A:ILE393 4.7 94.1 1.0 NE2 A:GLN325 4.8 82.5 1.0 C A:GLN325 4.9 96.2 1.0 CG A:GLN325 4.9 88.2 1.0 CA A:CYS323 4.9 83.8 1.0 C A:CYS394 5.0 100.4 1.0 N A:GLN325 5.0 96.0 1.0

A.Kroupova, V.Spiteri, H.Furihata, D.Darren, S.Ramachandran, Z.J.Rutter, S.Chakraborti, K.Haubrich, J.Pethe, D.Gonzales, A.Wijaya, M.Rodriguez-Rios, D.Lynch, W.Farnaby, M.Nakasone, D.Zollman, A.Ciulli. Design of A Cereblon Construct For Crystallographic and Biophysical Studies of Protein Degraders To Be Published.