Calcium 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
Sodium	(Na)	2 atoms

The binding sites of Calcium 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 Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Catalytic Domain of the Modular Laminarinase Zglamc Mutant E142S, PDB code: 4crq:
Jump to Calcium binding site number: 1; 2;

Calcium 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 Calcium with other atoms in the Ca 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 A:Ca260 b:24.2 occ:1.00 O A:GLY70 2.3 22.6 1.0 O A:GLU32 2.3 20.1 1.0 O A:HOH2013 2.3 25.4 1.0 OD1 A:ASP247 2.4 22.7 1.0 O A:ASP247 2.4 18.9 1.0 O A:HOH2073 2.5 32.0 1.0 O A:HOH2014 2.6 33.3 1.0 C A:GLY70 3.4 22.1 1.0 C A:ASP247 3.4 18.0 1.0 C A:GLU32 3.5 19.0 1.0 CG A:ASP247 3.6 22.1 1.0 CA A:ASP247 3.9 18.3 1.0 CA A:GLY70 4.0 22.6 1.0 O A:HOH2186 4.0 37.2 1.0 CA A:GLU32 4.2 19.1 1.0 CB A:ASP247 4.3 21.0 1.0 CB A:GLU32 4.5 21.4 1.0 O A:PHE33 4.5 24.5 1.0 OD2 A:ASP247 4.5 22.8 1.0 C A:PHE33 4.5 21.8 1.0 N A:ASN71 4.5 21.0 1.0 N A:PHE33 4.5 19.3 1.0 N A:TYR248 4.6 18.9 1.0 CB A:PHE33 4.6 20.6 1.0 OE1 A:GLU32 4.7 25.1 1.0 OD1 A:ASP34 4.7 37.8 1.0 CB A:TYR248 4.7 18.7 1.0 CA A:PHE33 4.8 20.6 1.0 CA A:ASN71 4.8 19.4 1.0 O A:HOH2187 4.8 48.8 1.0 N A:ASP34 4.9 23.9 1.0 CA A:TYR248 4.9 18.9 1.0

Calcium 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 Calcium with other atoms in the Ca 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:Ca260 b:23.4 occ:1.00 O B:GLY70 2.3 23.8 1.0 O B:HOH2018 2.4 23.5 1.0 O B:GLU32 2.4 20.2 1.0 OD1 B:ASP247 2.4 23.0 1.0 O B:ASP247 2.4 19.2 1.0 O B:HOH2088 2.4 33.1 1.0 O B:HOH2019 2.6 32.8 1.0 C B:ASP247 3.4 17.6 1.0 C B:GLY70 3.4 22.0 1.0 C B:GLU32 3.5 19.7 1.0 CG B:ASP247 3.6 22.9 1.0 CA B:ASP247 3.9 18.3 1.0 CA B:GLY70 4.0 23.5 1.0 O A:HOH2138 4.2 44.6 1.0 CA B:GLU32 4.2 19.7 1.0 O B:PHE33 4.3 26.9 1.0 CB B:ASP247 4.3 20.4 1.0 C B:PHE33 4.4 22.9 1.0 OD2 B:ASP247 4.5 25.1 1.0 N B:ASN71 4.5 24.1 1.0 N B:TYR248 4.5 18.8 1.0 CB B:GLU32 4.6 22.2 1.0 N B:PHE33 4.6 20.9 1.0 CB B:PHE33 4.6 20.5 1.0 OE1 B:GLU32 4.7 25.0 1.0 CB B:TYR248 4.7 19.3 1.0 OD1 B:ASP34 4.7 30.2 1.0 CA B:PHE33 4.8 20.0 1.0 CA B:ASN71 4.8 21.7 1.0 N B:ASP34 4.9 22.2 1.0 CA B:TYR248 4.9 19.3 1.0 CD2 B:TYR248 4.9 19.6 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