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Zinc in PDB 6bn7: Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac.

Protein crystallography data

The structure of Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac., PDB code: 6bn7 was solved by R.P.Nowak, S.L.Deangelo, D.Buckley, J.E.Bradner, E.S.Fischer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.87 / 3.50
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 115.571, 115.571, 596.315, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 25.6

Other elements in 6bn7:

The structure of Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. (pdb code 6bn7). 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 DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac., PDB code: 6bn7:

Zinc binding site 1 out of 1 in 6bn7

Go back to Zinc Binding Sites List in 6bn7
Zinc binding site 1 out of 1 in the Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac.


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 DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:0.7
occ:1.00
SG B:CYS391 2.3 0.1 1.0
SG B:CYS323 2.3 0.1 1.0
SG B:CYS394 2.4 0.8 1.0
SG B:CYS326 2.4 0.8 1.0
CB B:CYS391 2.8 0.6 1.0
CB B:CYS323 2.9 0.7 1.0
CB B:CYS326 3.1 0.3 1.0
CB B:CYS394 3.7 0.0 1.0
N B:CYS326 3.9 0.6 1.0
N B:CYS394 3.9 0.6 1.0
CA B:CYS326 4.1 0.3 1.0
CA B:CYS391 4.3 0.5 1.0
CA B:CYS394 4.3 0.1 1.0
CA B:CYS323 4.5 0.6 1.0
CB B:THR329 4.5 0.5 1.0
OG1 B:THR329 4.6 0.3 1.0
CG2 B:THR329 4.8 0.3 1.0
C B:GLN325 4.8 0.3 1.0
CB B:GLN325 4.9 0.6 1.0
CB B:SER396 4.9 0.1 1.0
CB B:ILE393 4.9 0.4 1.0
C B:CYS394 4.9 0.1 1.0
OG B:SER396 4.9 0.3 1.0
N B:ALA395 5.0 0.7 1.0
CD1 B:ILE398 5.0 0.0 1.0
C B:CYS391 5.0 0.5 1.0
N B:ILE393 5.0 0.6 1.0

Reference:

R.P.Nowak, S.L.Deangelo, D.Buckley, Z.He, K.A.Donovan, J.An, N.Safaee, M.P.Jedrychowski, C.M.Ponthier, M.Ishoey, T.Zhang, J.D.Mancias, N.S.Gray, J.E.Bradner, E.S.Fischer. Plasticity in Binding Confers Selectivity in Ligand-Induced Protein Degradation. Nat. Chem. Biol. V. 14 706 2018.
ISSN: ESSN 1552-4469
PubMed: 29892083
DOI: 10.1038/S41589-018-0055-Y
Page generated: Wed Dec 16 11:32:40 2020

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