Sodium in PDB 2wrx: Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0

The structure of Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0, PDB code: 2wrx was solved by A.M.Brzozowski, J.Jiracek, L.Zakova, E.Antolikova, C.J.Watson, J.P.Turkenburg, G.G.Dodson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.42 / 1.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	39.239, 39.239, 124.908, 90.00, 90.00, 90.00
R / Rfree (%)	18.019 / 25.053

The binding sites of Sodium atom in the Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0 (pdb code 2wrx). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0, PDB code: 2wrx:

Sodium binding site 1 out of 1 in the Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Semi-Synthetic Analogue of Human Insulin NMEALAB26-Insulin at pH 3.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na2000 b:35.4 occ:1.00 O D:HOH2026 2.6 22.3 1.0 O B:HOH2019 3.1 24.6 1.0 O A:HOH2001 3.1 15.4 1.0 O C:HOH2002 3.3 13.1 1.0 CD1 A:TYR19 3.8 16.4 1.0 CD2 C:TYR19 3.8 12.1 1.0 CG2 A:ILE2 4.3 13.6 1.0 CG2 C:ILE2 4.3 12.4 1.0 CE1 A:TYR19 4.5 15.7 1.0 CE2 C:TYR19 4.5 17.1 1.0 CG C:TYR19 4.5 15.6 1.0 CG A:TYR19 4.6 15.0 1.0 CB C:TYR19 4.6 16.1 1.0 CB A:TYR19 4.6 16.2 1.0 CD2 B:PHE25 4.6 11.1 1.0 CB A:ILE2 4.6 12.9 1.0 CB C:ILE2 4.7 9.3 1.0 CD2 D:PHE25 4.8 10.9 1.0 O C:TYR19 4.8 16.9 1.0 O C:HOH2024 4.9 11.2 1.0 O A:TYR19 4.9 16.4 1.0 O A:HOH2023 4.9 13.2 1.0

J.Jiracek, L.Zakova, E.Antolikova, C.J.Watson, J.P.Turkenburg, G.G.Dodson, A.M.Brzozowski. Implications For the Active Form of Human Insulin Based on the Structural Convergence of Highly Active Hormone Analogues. Proc.Natl.Acad.Sci.Usa V. 107 1966 2010.
ISSN: ISSN 0027-8424
PubMed: 20133841
DOI: 10.1073/PNAS.0911785107