Zinc in PDB 2omh: Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea

The structure of Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea, PDB code: 2omh was solved by M.Norrman, G.Schluckebier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.95 / 1.36
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.360, 61.360, 85.600, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 22.3

The structure of Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom

The binding sites of Zinc atom in the Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea (pdb code 2omh). 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 Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea, PDB code: 2omh:

Zinc binding site 1 out of 1 in the Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Insulin Cocrystallized with Arg-12 Peptide in Presence of Urea within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:12.5 occ:1.00 NE2 B:HIS10 2.0 14.8 1.0 NE2 D:HIS10 2.0 15.3 1.0 NE2 F:HIS10 2.0 14.6 1.0 CL B:CL301 2.1 19.0 1.0 CE1 B:HIS10 3.0 17.6 1.0 CD2 D:HIS10 3.0 14.1 1.0 CD2 B:HIS10 3.0 13.3 1.0 CE1 D:HIS10 3.0 17.9 1.0 CD2 F:HIS10 3.0 15.0 1.0 CE1 F:HIS10 3.0 16.8 1.0 O B:HOH320 4.0 38.6 1.0 ND1 B:HIS10 4.1 18.2 1.0 ND1 D:HIS10 4.1 19.1 1.0 CG D:HIS10 4.1 15.2 1.0 ND1 F:HIS10 4.1 16.8 1.0 CG B:HIS10 4.1 13.8 1.0 CG F:HIS10 4.2 15.4 1.0 O D:LEU6 4.7 15.4 1.0 O B:LEU6 4.7 14.5 1.0 O B:HOH319 4.8 34.4 1.0 CB D:LEU6 4.8 15.1 1.0 CB B:LEU6 4.8 14.3 1.0 O F:LEU6 4.8 15.7 1.0 CB F:LEU6 4.8 15.9 1.0 O B:HOH308 4.9 35.3 1.0 O D:HOH705 4.9 33.4 1.0

M.Norrman, F.Hubalek, G.Schluckebier. Structural Characterization of Insulin Nph Formulations. Eur.J.Pharm.Sci. V. 30 414 2007.
PubMed: 17339105
DOI: 10.1016/J.EJPS.2007.01.003