Zinc in PDB 1lph: Lys(B28)Pro(B29)-Human Insulin

The structure of Lys(B28)Pro(B29)-Human Insulin, PDB code: 1lph was solved by E.Ciszak, J.M.Beals, B.H.Frank, J.C.Baker, N.D.Carter, G.D.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	79.620, 79.620, 37.780, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of Lys(B28)Pro(B29)-Human Insulin also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Lys(B28)Pro(B29)-Human Insulin (pdb code 1lph). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Lys(B28)Pro(B29)-Human Insulin, PDB code: 1lph:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Lys(B28)Pro(B29)-Human Insulin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Lys(B28)Pro(B29)-Human Insulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn31 b:25.6 occ:0.33 NE2 B:HIS10 2.2 25.6 1.0 CE1 B:HIS10 3.1 25.2 1.0 CD2 B:HIS10 3.2 24.9 1.0 O B:HOH32 3.5 51.0 1.0 ND1 B:HIS10 4.2 25.5 1.0 CG B:HIS10 4.3 25.9 1.0

Zinc binding site 2 out of 2 in the Lys(B28)Pro(B29)-Human Insulin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Lys(B28)Pro(B29)-Human Insulin within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn31 b:21.7 occ:0.33 NE2 D:HIS10 2.0 17.7 1.0 CL D:CL32 2.3 36.7 0.3 CE1 D:HIS10 2.9 20.2 1.0 CD2 D:HIS10 3.2 17.8 1.0 ND1 D:HIS10 4.1 20.0 1.0 CG D:HIS10 4.2 19.0 1.0 O D:LEU6 4.5 27.2 1.0 CB D:LEU6 4.8 23.4 1.0

E.Ciszak, J.M.Beals, B.H.Frank, J.C.Baker, N.D.Carter, G.D.Smith. Role of C-Terminal B-Chain Residues in Insulin Assembly: the Structure of Hexameric LYSB28PROB29-Human Insulin. Structure V. 3 615 1995.
ISSN: ISSN 0969-2126
PubMed: 8590022
DOI: 10.1016/S0969-2126(01)00195-2