Chlorine in PDB 1zeh: Structure of Insulin

The structure of Structure of Insulin, PDB code: 1zeh was solved by J.L.Whittingham, E.J.Edwards, A.A.Antson, J.M.Clarkson, G.G.Dodson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.40 / 1.50
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	77.490, 77.490, 38.910, 90.00, 90.00, 120.00
R / Rfree (%)	15.9 / 19.3

The structure of Structure of Insulin also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Structure of Insulin (pdb code 1zeh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Insulin, PDB code: 1zeh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Insulin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Insulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl32 b:14.5 occ:0.33 ZN B:ZN31 2.2 13.1 0.3 NE2 B:HIS10 3.5 11.7 1.0 CB B:LEU6 3.8 15.6 1.0 CD2 B:HIS10 4.0 10.8 1.0 CD1 B:LEU6 4.2 19.9 1.0 CG B:LEU6 4.4 16.3 1.0 CD2 B:LEU6 4.5 20.6 1.0 CE1 B:HIS10 4.5 15.3 1.0 O B:LEU6 4.8 13.9 1.0 CA B:LEU6 4.8 13.2 1.0 C B:LEU6 4.9 13.9 1.0

Chlorine binding site 2 out of 2 in the Structure of Insulin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Insulin within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl32 b:12.1 occ:0.33 ZN D:ZN31 2.2 12.1 0.3 NE2 D:HIS10 3.4 10.2 1.0 CB D:LEU6 3.8 14.4 1.0 CD2 D:HIS10 3.9 11.5 1.0 CD1 D:LEU6 4.0 19.1 1.0 CG D:LEU6 4.2 18.1 1.0 CD2 D:LEU6 4.3 21.2 1.0 CE1 D:HIS10 4.5 14.1 1.0 CA D:LEU6 4.7 13.4 1.0 O D:LEU6 4.7 12.2 1.0 C D:LEU6 4.9 12.1 1.0 CG D:HIS10 5.0 11.7 1.0

J.L.Whittingham, D.J.Edwards, A.A.Antson, J.M.Clarkson, G.G.Dodson. Interactions of Phenol and M-Cresol in the Insulin Hexamer, and Their Effect on the Association Properties of B28 Pro --> Asp Insulin Analogues. Biochemistry V. 37 11516 1998.
ISSN: ISSN 0006-2960
PubMed: 9708987
DOI: 10.1021/BI980807S