Sodium in PDB 4crq: Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S

All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S:
3.2.1.39;

The structure of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S, PDB code: 4crq was solved by A.Labourel, M.Jam, L.Legentil, B.Sylla, E.Ficko-Blean, J.H.Hehemann, V.Ferrieres, M.Czjzek, G.Michel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.98 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.108, 68.061, 143.282, 90.00, 90.00, 90.00
R / Rfree (%)	14.802 / 18.576

The structure of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Chlorine	(Cl)	3 atoms
Calcium	(Ca)	2 atoms

The binding sites of Sodium atom in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S (pdb code 4crq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S, PDB code: 4crq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S


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 Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1260 b:26.3 occ:1.00 O B:PRO175 2.7 18.6 1.0 OH B:TYR181 2.8 17.0 1.0 O B:ILE108 2.8 17.2 1.0 O B:GLN177 3.2 18.3 1.0 CE2 B:TYR181 3.4 16.9 1.0 CZ B:TYR181 3.5 17.3 1.0 C B:PRO175 3.6 18.7 1.0 CD2 B:HIS179 3.7 19.6 1.0 C B:ILE108 3.7 17.0 1.0 CG B:LEU110 3.8 16.6 1.0 CA B:PRO175 3.9 21.1 1.0 CA B:ALA109 3.9 18.3 1.0 N B:LEU110 3.9 16.6 1.0 CB B:HIS179 3.9 17.9 1.0 CD1 B:LEU110 4.0 21.0 1.0 N B:HIS179 4.0 17.9 1.0 CG B:HIS179 4.1 19.6 1.0 N B:ALA109 4.2 16.8 1.0 C B:ALA109 4.2 16.3 1.0 CB B:LEU110 4.4 18.3 1.0 CB B:PRO175 4.4 19.9 1.0 C B:GLN177 4.4 18.4 1.0 CA B:HIS179 4.5 18.5 1.0 C B:TYR178 4.6 17.8 1.0 O B:HIS179 4.7 25.3 1.0 CD2 B:TYR181 4.8 17.2 1.0 CB B:ILE108 4.8 16.6 1.0 CA B:LEU110 4.8 17.1 1.0 CG2 B:ILE108 4.8 17.2 1.0 CA B:TYR178 4.8 18.4 1.0 CA B:ILE108 4.8 16.3 1.0 N B:GLY176 4.9 20.5 1.0 NE2 B:HIS179 4.9 22.3 1.0 CE1 B:TYR181 4.9 18.1 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1262 b:41.3 occ:1.00 OE1 B:GLN94 3.6 24.9 1.0 OE2 B:GLU44 3.6 22.8 0.5 O B:HOH2109 3.9 27.2 1.0 NZ B:LYS92 3.9 22.0 1.0 CZ B:PHE219 4.0 17.6 1.0 OE2 B:GLU44 4.0 24.4 0.5 CD1 B:LEU123 4.2 17.1 1.0 NH2 B:ARG90 4.2 20.0 1.0 CD B:LYS92 4.2 19.6 1.0 CD B:GLN94 4.3 20.6 1.0 CE1 B:PHE219 4.4 18.8 1.0 CD B:GLU44 4.5 23.8 0.5 NE2 B:GLN94 4.5 23.3 1.0 CD1 B:ILE127 4.6 19.9 1.0 OE1 B:GLU44 4.7 25.7 0.5 O B:HOH2106 4.7 40.8 1.0 CE B:LYS92 4.7 21.0 1.0 CD2 B:LEU221 4.8 17.5 1.0 O B:HOH2039 4.9 42.3 1.0

A.Labourel, M.Jam, L.Legentil, B.Sylla, J.H.Hehemann, V.Ferrieres, M.Czjzek, G.Michel. Structural and Biochemical Characterization of the Laminarina Zglamc[GH16] From Zobellia Galactanivorans Suggests Preferred Recognition of Branched Laminarin Acta Crystallogr.,Sect.D V. 71 173 2015.
ISSN: ISSN 0907-4449
DOI: 10.1107/S139900471402450X