Sodium in PDB 1pqh: Serine 25 to Threonine Mutation of Aspartate Decarboxylase

All present enzymatic activity of Serine 25 to Threonine Mutation of Aspartate Decarboxylase:
4.1.1.11;

The structure of Serine 25 to Threonine Mutation of Aspartate Decarboxylase, PDB code: 1pqh was solved by F.Schmitzberger, M.L.Kilkenny, C.M.C.Lobley, M.E.Webb, M.Vinkovic, D.Matak-Vinkovic, M.Witty, D.Y.Chirgadze, A.G.Smith, C.Abell, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.71 / 1.29
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	70.460, 70.460, 215.299, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 16.6

The binding sites of Sodium atom in the Serine 25 to Threonine Mutation of Aspartate Decarboxylase (pdb code 1pqh). 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 Serine 25 to Threonine Mutation of Aspartate Decarboxylase, PDB code: 1pqh:

Sodium binding site 1 out of 1 in the Serine 25 to Threonine Mutation of Aspartate Decarboxylase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Serine 25 to Threonine Mutation of Aspartate Decarboxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Na393 b:29.0 occ:1.00 O A:HOH539 2.3 18.0 1.0 NZ A:LYS14 3.3 25.6 1.0 CE A:LYS14 3.5 23.4 1.0 O A:HOH493 3.7 16.8 1.0 CD1 A:ILE84 4.0 18.4 1.0 CG1 A:ILE84 4.7 15.6 1.0 O A:HOH411 4.8 28.1 1.0

F.Schmitzberger, M.L.Kilkenny, C.M.C.Lobley, M.E.Webb, M.Vinkovic, D.Matak-Vinkovic, M.Witty, D.Y.Chirgadze, A.G.Smith, C.Abell, T.L.Blundell. Structural Constraints on Protein Self-Processing in L-Aspartate-Alpha-Decarboxylase Embo J. V. 22 6193 2003.
ISSN: ISSN 0261-4189
PubMed: 14633979
DOI: 10.1093/EMBOJ/CDG575