Chlorine in PDB 7bmc: Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A

The structure of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A, PDB code: 7bmc was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.30 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	83.716, 111.429, 62.61, 90, 90, 90
R / Rfree (%)	18.3 / 22

The structure of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A (pdb code 7bmc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A, PDB code: 7bmc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:11.5 occ:1.00 HZ3 A:LYS9 2.2 9.0 1.0 HD3 A:LYS9 3.0 7.2 1.0 NZ A:LYS9 3.1 7.5 1.0 HZ2 A:LYS9 3.4 9.0 1.0 HZ1 A:LYS9 3.5 9.0 1.0 HE2 A:LYS9 3.7 6.5 1.0 CE A:LYS9 3.7 5.4 1.0 HZ A:PHE25 3.8 10.1 1.0 CD A:LYS9 3.8 5.9 1.0 HE1 A:MET1 3.9 11.3 1.0 HE1 A:PHE25 4.1 8.3 1.0 HD2 A:LYS9 4.2 7.2 1.0 HE2 A:MET1 4.3 11.3 1.0 CZ A:PHE25 4.4 8.4 1.0 CE A:MET1 4.5 9.4 1.0 CE1 A:PHE25 4.6 6.9 1.0 HE3 A:LYS9 4.6 6.5 1.0 HG2 A:LYS9 4.8 6.8 1.0 O A:HOH626 4.8 30.6 1.0 O A:HOH706 4.9 32.8 1.0 CG A:LYS9 4.9 5.7 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of 14-3-3 Sigma in Complex with CIP2APS904 Peptide and Stabilizing Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1001 b:19.3 occ:1.00 H271 A:FSC301 2.7 10.9 1.0 O A:HOH536 2.8 8.8 1.0 O A:HOH531 2.8 5.7 1.0 OXT B:ILE905 2.8 8.1 1.0 HZ2 A:LYS122 2.8 7.1 1.0 HD2 A:LYS49 3.0 21.6 1.0 HZ1 A:LYS122 3.1 7.1 1.0 H20 A:FSC301 3.2 7.8 1.0 H5 A:FSC301 3.2 9.2 1.0 NZ A:LYS122 3.3 5.9 1.0 C27 A:FSC301 3.4 9.1 1.0 H383 A:FSC301 3.4 9.8 1.0 O B:ILE905 3.4 7.8 1.0 O32 A:FSC301 3.4 9.4 1.0 HB2 A:SER45 3.4 6.3 1.0 HZ3 A:LYS122 3.5 7.1 1.0 C B:ILE905 3.5 8.8 1.0 C20 A:FSC301 3.7 6.5 1.0 HZ1 A:LYS49 3.8 25.1 1.0 C38 A:FSC301 3.9 8.1 1.0 CD A:LYS49 4.0 18.0 1.0 HB2 A:LYS49 4.0 8.1 1.0 O B:HOH1103 4.0 12.3 1.0 C5 A:FSC301 4.1 7.6 1.0 O A:HOH475 4.1 5.7 1.0 H272 A:FSC301 4.2 10.9 1.0 CB A:SER45 4.3 5.2 1.0 H13 A:FSC301 4.3 8.5 1.0 HD3 A:LYS49 4.3 21.6 1.0 C12 A:FSC301 4.4 7.9 1.0 OD2 A:ASP126 4.4 6.2 1.0 OG A:SER45 4.5 6.8 1.0 H382 A:FSC301 4.5 9.8 1.0 HE3 A:LYS49 4.5 25.3 1.0 H381 A:FSC301 4.6 9.8 1.0 O13 A:FSC301 4.6 7.0 1.0 NZ A:LYS49 4.6 20.9 1.0 CE A:LYS49 4.6 21.1 1.0 CE A:LYS122 4.7 6.9 1.0 CB A:LYS49 4.7 6.7 1.0 HD21 A:ASN175 4.8 9.1 1.0 CG A:LYS49 4.8 10.0 1.0 HG3 A:LYS49 4.8 12.1 1.0 HE3 A:LYS122 4.8 8.3 1.0 HG23 B:ILE905 4.8 9.1 1.0 HB3 A:SER45 4.9 6.3 1.0 O A:SER45 4.9 6.6 1.0 HG13 B:ILE905 4.9 11.5 1.0 HZ3 A:LYS49 4.9 25.1 1.0 HB3 A:LYS49 5.0 8.1 1.0

H.J.Brink, J.R.Van Senten, I.J.De Vries-Van Leeuwen, D.Da Costa Pereira, S.R.Piersma, C.R.Jimenez, F.Centorrino, C.Ottmann, M.Siderius, M.J.Smit, A.H.De Boer. Fusicoccin-A Targets Cancerous Inhibitor of Protein Phosphatase 2A By Stabilizing A C-Terminal Interaction with 14-3-3. Acs Chem.Biol. V. 17 2972 2022.
ISSN: ESSN 1554-8937
PubMed: 36255265
DOI: 10.1021/ACSCHEMBIO.2C00299