Zinc in PDB 4efx: Highly Biologically Active Insulin with Additional Disulfide Bond

The structure of Highly Biologically Active Insulin with Additional Disulfide Bond, PDB code: 4efx was solved by M.Norrman, T.N.Vinther, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.69 / 1.98
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	79.367, 79.367, 34.228, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 27.8

The binding sites of Zinc atom in the Highly Biologically Active Insulin with Additional Disulfide Bond (pdb code 4efx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Highly Biologically Active Insulin with Additional Disulfide Bond, PDB code: 4efx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Highly Biologically Active Insulin with Additional Disulfide Bond


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Highly Biologically Active Insulin with Additional Disulfide Bond within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn101 b:23.8 occ:0.33 NE2 B:HIS10 2.1 18.4 1.0 CD2 B:HIS10 3.1 17.0 1.0 CE1 B:HIS10 3.1 18.1 1.0 ND1 B:HIS10 4.2 16.3 1.0 CG B:HIS10 4.2 14.6 1.0 O B:HOH202 5.0 37.4 1.0

Zinc binding site 2 out of 2 in the Highly Biologically Active Insulin with Additional Disulfide Bond


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Highly Biologically Active Insulin with Additional Disulfide Bond within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn101 b:26.2 occ:0.33 NE2 D:HIS10 2.1 14.1 1.0 CE1 D:HIS10 2.9 12.5 1.0 O D:HOH213 2.9 5.2 0.3 CD2 D:HIS10 3.3 13.9 1.0 O D:HOH209 3.8 27.8 0.3 ND1 D:HIS10 4.1 12.7 1.0 CG D:HIS10 4.3 13.7 1.0 OG D:SER9 4.8 14.8 1.0

T.N.Vinther, M.Norrman, U.Ribel, K.Huus, M.Schlein, D.B.Steensgaard, T.A.Pedersen, I.Pettersson, S.Ludvigsen, T.Kjeldsen, K.J.Jensen, F.Hubalek. Insulin Analog with Additional Disulfide Bond Has Increased Stability and Preserved Activity. Protein Sci. V. 22 296 2013.
ISSN: ISSN 0961-8368
PubMed: 23281053
DOI: 10.1002/PRO.2211