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Sodium in PDB 4bow: Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose

Enzymatic activity of Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose

All present enzymatic activity of Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose:
3.2.1.39;

Protein crystallography data

The structure of Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose, PDB code: 4bow was solved by A.Labourel, A.Jeudy, M.Czjzek, G.Michel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.44 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.459, 76.495, 142.941, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 16.666

Other elements in 4bow:

The structure of Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose (pdb code 4bow). 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 LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose, PDB code: 4bow:

Sodium binding site 1 out of 1 in 4bow

Go back to Sodium Binding Sites List in 4bow
Sodium binding site 1 out of 1 in the Crystal Structure of LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose


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 LAMA_E269S From Z. Galactanivorans in Complex with Laminaritriose and Laminaritetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na399

b:35.6
occ:1.00
OD1 B:ASP295 2.5 28.0 1.0
O B:HOH2151 2.7 37.9 1.0
OG B:SER290 2.8 18.2 0.5
CB B:SER290 3.3 18.2 0.5
OG B:SER290 3.5 27.8 0.5
CG B:ASP295 3.5 28.1 1.0
CA B:ASP295 3.5 18.6 1.0
CB B:SER290 3.6 20.4 0.5
CB B:ASP295 3.8 22.6 1.0
CB B:ALA266 3.8 22.3 1.0
CD2 B:LEU292 4.1 22.7 1.0
O A:HOH2187 4.2 40.2 1.0
CE1 B:TYR297 4.2 31.9 1.0
C B:ASP295 4.4 20.6 1.0
N B:ASP295 4.5 17.3 1.0
O B:HOH2097 4.5 40.1 1.0
O B:ASP291 4.6 17.1 1.0
CA B:LEU292 4.6 17.6 1.0
O B:ASP295 4.7 24.4 1.0
CA B:ALA266 4.7 17.7 1.0
OD2 B:ASP295 4.7 27.9 1.0
CA B:SER290 4.8 17.4 0.5
O B:HOH2127 4.8 50.6 1.0
CD1 B:TYR297 4.8 26.3 1.0
CA B:SER290 4.9 17.2 0.5
O B:LEU292 5.0 20.0 1.0

Reference:

A.Labourel, M.Jam, A.Jeudy, J.H.Hehemann, M.Czjzek, G.Michel. The Beta-Glucanase Zglama From Zobellia Galactanivorans Evolved A Bent Active Site Adapted For Efficient Degradation of Algal Laminarin J.Biol.Chem. V. 289 2027 2014.
ISSN: ISSN 0021-9258
PubMed: 24337571
DOI: 10.1074/JBC.M113.538843
Page generated: Tue Dec 15 06:34:43 2020

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