Zinc in PDB 1w8p: Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant.

The structure of Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant., PDB code: 1w8p was solved by L.Zakowa, O.Au-Alvarez, E.J.Dodson, G.G.Dodson, A.M.Brzozowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.57 / 2.08
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.903, 62.116, 47.796, 90.00, 110.58, 90.00
R / Rfree (%)	18.9 / 25.6

The binding sites of Zinc atom in the Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant. (pdb code 1w8p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant., PDB code: 1w8p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1030 b:27.9 occ:1.00 NE2 B:HIS10 2.0 27.1 1.0 NE2 F:HIS10 2.1 24.0 1.0 NE2 J:HIS10 2.1 25.4 1.0 O B:HOH2009 2.2 16.6 1.0 CE1 B:HIS10 3.0 29.1 1.0 CE1 J:HIS10 3.0 30.1 1.0 CD2 B:HIS10 3.0 29.3 1.0 CE1 F:HIS10 3.0 28.2 1.0 CD2 F:HIS10 3.1 25.6 1.0 CD2 J:HIS10 3.1 25.8 1.0 ND1 B:HIS10 4.1 30.5 1.0 CG B:HIS10 4.1 28.3 1.0 ND1 J:HIS10 4.1 27.1 1.0 ND1 F:HIS10 4.1 24.6 1.0 CG F:HIS10 4.2 27.0 1.0 CG J:HIS10 4.2 27.6 1.0 O F:LEU6 4.5 28.7 1.0 O B:LEU6 4.8 24.8 1.0 CB F:LEU6 4.8 30.0 1.0 O J:LEU6 4.9 27.4 1.0 CB B:LEU6 5.0 24.6 1.0

Zinc binding site 2 out of 2 in the Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant. within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1030 b:26.6 occ:1.00 CE1 D:HIS10 1.8 25.1 1.0 NE2 L:HIS10 2.0 20.7 1.0 NE2 H:HIS10 2.1 24.2 1.0 O D:HOH2012 2.2 17.6 1.0 NE2 D:HIS10 2.2 26.7 1.0 CE1 H:HIS10 2.9 27.5 1.0 CE1 L:HIS10 3.0 23.3 1.0 CD2 L:HIS10 3.1 24.0 1.0 ND1 D:HIS10 3.1 29.7 1.0 CD2 H:HIS10 3.2 25.9 1.0 CD2 D:HIS10 3.6 25.7 1.0 CG D:HIS10 4.0 26.9 1.0 ND1 H:HIS10 4.1 29.2 1.0 ND1 L:HIS10 4.1 22.5 1.0 CG L:HIS10 4.2 25.3 1.0 CG H:HIS10 4.2 26.6 1.0 O L:LEU6 4.6 31.9 1.0 CB L:LEU6 4.9 31.8 1.0 O D:LEU6 4.9 31.6 1.0 CB H:LEU6 4.9 26.0 1.0 O H:LEU6 4.9 27.3 1.0 O H:HOH2003 5.0 59.7 1.0

L.Zarkowa, J.Brynda, O.Au-Alvarez, E.J.Dodson, G.G.Dodson, J.L.Whittingham, A.M.Brzozowski. Towards the Insulin-Igf-I Intermediate Structures: Functional and Structural Properties of the B25TYR-Nme-B26PHE Insulin Mutant. Biochemistry V. 43 16293 2004.
ISSN: ISSN 0006-2960
PubMed: 15610023
DOI: 10.1021/BI048856U