Sodium in PDB 3umb: Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362

All present enzymatic activity of Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362:
3.8.1.2;

The structure of Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362, PDB code: 3umb was solved by P.Petit, P.W.Y.Chan, A.Savchenko, A.F.Yakunin, E.A.Edwards, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.67 / 2.20
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	66.380, 129.570, 54.300, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 28.3

The structure of Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362 also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Potassium	(K)	2 atoms
Chlorine	(Cl)	3 atoms

The binding sites of Sodium atom in the Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362 (pdb code 3umb). 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 Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362, PDB code: 3umb:

Sodium binding site 1 out of 1 in the Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the L-2-Haloacid Dehalogenase RSC1362 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na239 b:26.7 occ:1.00 O A:HOH285 2.9 29.6 1.0 NE2 A:HIS191 3.0 25.4 1.0 O A:HOH273 3.1 23.3 1.0 CG A:PRO165 3.5 24.6 1.0 CB A:PRO165 3.7 25.7 1.0 CE1 A:HIS191 3.7 26.2 1.0 CA A:ALA162 3.8 19.8 1.0 CB A:ALA162 3.9 18.8 1.0 CD2 A:HIS191 4.1 25.4 1.0 CD A:PRO165 4.2 25.4 1.0 O A:ALA162 4.3 21.1 1.0 C A:ALA162 4.6 20.0 1.0 N A:ALA162 4.8 19.8 1.0 ND1 A:HIS191 4.9 24.4 1.0

P.W.Y.Chan, T.K.W.To, P.Petit, C.Tran, M.Waelti, A.Savchenko, A.F.Yakunin, E.A.Edwards, E.F.Pai. Structural Adaptations of L-2-Haloacid Dehalogenases That Enable Hydrolytic Defluorination To Be Published.