Chlorine in PDB 9hix: Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1

All present enzymatic activity of Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1:
2.7.11.22; 2.7.11.23;

The binding sites of Chlorine atom in the Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1 (pdb code 9hix). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1, PDB code: 9hix:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1 within 5.0Å range: probe atom residue distance (Å) B Occ J:Cl401 b:22.6 occ:0.81 CL01 J:V0G401 0.0 22.6 0.8 C02 J:V0G401 1.8 15.0 0.8 C03 J:V0G401 2.7 15.1 0.8 C32 J:V0G401 2.8 14.9 0.8 C34 J:V0G401 3.1 14.2 0.8 C33 J:V0G401 3.2 13.7 0.8 CD1 J:PHE91 3.4 18.6 1.0 CG J:PHE91 3.7 17.3 1.0 CB J:PHE91 3.9 18.8 1.0 N04 J:V0G401 4.0 14.0 0.8 N31 J:V0G401 4.0 16.0 0.8 CE1 J:PHE91 4.1 20.4 1.0 N35 J:V0G401 4.3 16.8 0.8 CD J:LYS41 4.4 31.4 1.0 CD2 J:PHE91 4.4 16.0 1.0 C05 J:V0G401 4.5 17.5 0.8 C41 J:V0G401 4.5 16.4 0.8 CD1 J:LEU144 4.6 10.9 1.0 CB J:ALA39 4.6 21.2 1.0 CG J:LYS41 4.6 32.8 1.0 CG1 J:VAL26 4.7 22.7 1.0 CZ J:PHE91 4.8 19.6 1.0 CE2 J:PHE91 4.9 16.4 1.0 C36 J:V0G401 5.0 18.0 0.8

Chlorine binding site 2 out of 2 in the Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cryo-Em Structure of Cak (CDK7 D97N Mutant) in Complex with THZ1 within 5.0Å range: probe atom residue distance (Å) B Occ J:Cl401 b:16.9 occ:0.19 CL01 J:V0G401 0.0 16.9 0.2 C02 J:V0G401 1.8 19.0 0.2 C03 J:V0G401 2.7 18.2 0.2 C32 J:V0G401 2.8 20.9 0.2 C34 J:V0G401 3.1 21.6 0.2 C33 J:V0G401 3.2 21.3 0.2 O J:ASN141 3.3 16.3 1.0 OD1 J:ASN142 3.4 23.6 1.0 C37 J:V0G401 3.5 17.8 0.8 C36 J:V0G401 3.6 18.0 0.8 OD1 J:ASN141 3.7 24.8 1.0 C J:ASN141 3.8 15.1 1.0 N35 J:V0G401 3.9 16.8 0.8 CB J:ASN141 4.0 19.6 1.0 OD2 J:ASP155 4.0 21.0 1.0 N04 J:V0G401 4.0 19.5 0.2 N31 J:V0G401 4.0 22.3 0.2 C38 J:V0G401 4.1 19.3 0.8 OD1 J:ASP155 4.2 19.3 1.0 C41 J:V0G401 4.3 16.4 0.8 CG J:ASP155 4.3 18.8 1.0 CG J:ASN141 4.3 25.5 1.0 N J:ASN142 4.3 13.8 1.0 N35 J:V0G401 4.3 23.2 0.2 CA J:ASN142 4.4 13.2 1.0 CG J:ASN142 4.5 18.6 1.0 C05 J:V0G401 4.5 22.0 0.2 CA J:ASN141 4.5 17.3 1.0 C41 J:V0G401 4.6 22.5 0.2 C34 J:V0G401 4.6 14.2 0.8 C39 J:V0G401 4.7 17.4 0.8 C40 J:V0G401 4.7 17.3 0.8 C33 J:V0G401 4.8 13.7 0.8

C.-F.Lai, V.I.Cushing, C.L.Bevan, R.C.Coombes, B.J.Greber, L.Buluwela, S.Ali. Mutation of CDK7 at A Conserved Residue Identifies A Common Mechanism of Acquired Resistance to Cdk Inhibitors in Cancer To Be Published.