Zinc in PDB 2omi: Structure of Human Insulin Cocrystallized with Protamine

The structure of Structure of Human Insulin Cocrystallized with Protamine, PDB code: 2omi 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)	29.10 / 2.24
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.520, 61.840, 86.000, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 26.8

The structure of Structure of Human Insulin Cocrystallized with Protamine also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

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

Zinc binding site 1 out of 2 in the Structure of Human Insulin Cocrystallized with Protamine


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 Protamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:13.6 occ:1.00 NE2 F:HIS10 2.0 12.5 1.0 NE2 B:HIS10 2.0 18.6 1.0 CL B:CL402 2.1 14.5 1.0 NE2 D:HIS10 2.1 12.2 1.0 CE1 B:HIS10 2.9 17.7 1.0 CD2 F:HIS10 2.9 14.8 1.0 CE1 F:HIS10 3.0 15.0 1.0 CE1 D:HIS10 3.0 13.6 1.0 CD2 B:HIS10 3.1 12.7 1.0 CD2 D:HIS10 3.1 15.4 1.0 ND1 B:HIS10 4.0 15.7 1.0 ND1 F:HIS10 4.1 17.1 1.0 CG F:HIS10 4.1 11.7 1.0 CG B:HIS10 4.1 13.9 1.0 ND1 D:HIS10 4.1 13.2 1.0 CG D:HIS10 4.2 13.8 1.0 O B:LEU6 4.6 14.7 1.0 CB F:LEU6 4.7 14.9 1.0 O F:LEU6 4.8 14.9 1.0 O D:LEU6 4.8 15.7 1.0 CB B:LEU6 4.9 12.7 1.0 CB D:LEU6 4.9 12.4 1.0

Zinc binding site 2 out of 2 in the Structure of Human Insulin Cocrystallized with Protamine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Insulin Cocrystallized with Protamine within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn201 b:15.6 occ:1.00 NE2 L:HIS10 1.9 15.0 1.0 NE2 J:HIS10 2.0 14.7 1.0 CL J:CL401 2.1 12.7 1.0 NE2 H:HIS10 2.2 19.5 1.0 CE1 L:HIS10 2.8 17.4 1.0 CE1 J:HIS10 2.8 11.2 1.0 CD2 L:HIS10 3.0 11.8 1.0 CD2 H:HIS10 3.1 14.9 1.0 CD2 J:HIS10 3.1 11.2 1.0 CE1 H:HIS10 3.3 19.8 1.0 ND1 L:HIS10 3.9 20.2 1.0 ND1 J:HIS10 4.0 9.6 1.0 CG L:HIS10 4.1 12.2 1.0 CG J:HIS10 4.2 12.4 1.0 CG H:HIS10 4.3 15.0 1.0 ND1 H:HIS10 4.3 20.0 1.0 O H:LEU6 4.5 17.1 1.0 O J:LEU6 4.6 15.3 1.0 O L:LEU6 4.8 16.0 1.0 CB L:LEU6 4.8 14.1 1.0 CB J:LEU6 4.8 12.9 1.0 CB H:LEU6 4.9 14.3 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