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Sodium in PDB 5m5z: Chaetomium Thermophilum Beta-1-3-Glucanase

Protein crystallography data

The structure of Chaetomium Thermophilum Beta-1-3-Glucanase, PDB code: 5m5z was solved by A.C.Papageorgiou, J.Chen, D.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.92 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.774, 85.277, 66.765, 90.00, 92.83, 90.00
R / Rfree (%) 12.3 / 14.1

Other elements in 5m5z:

The structure of Chaetomium Thermophilum Beta-1-3-Glucanase also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Chaetomium Thermophilum Beta-1-3-Glucanase (pdb code 5m5z). 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 Chaetomium Thermophilum Beta-1-3-Glucanase, PDB code: 5m5z:

Sodium binding site 1 out of 1 in 5m5z

Go back to Sodium Binding Sites List in 5m5z
Sodium binding site 1 out of 1 in the Chaetomium Thermophilum Beta-1-3-Glucanase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Chaetomium Thermophilum Beta-1-3-Glucanase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na809

b:18.9
occ:0.63
O A:HOH1368 2.4 42.5 1.0
O A:ASP436 2.6 15.1 1.0
O A:HOH1747 2.6 30.0 1.0
O A:HOH1120 2.6 45.9 1.0
O A:HOH1195 2.6 12.4 1.0
O A:HOH1700 3.1 44.4 1.0
C A:ASP436 3.6 13.2 1.0
O A:HOH2044 3.8 40.2 1.0
O A:HOH1220 4.0 13.9 1.0
O A:HOH1771 4.2 38.6 1.0
CA A:ASP436 4.3 11.6 1.0
N A:SER437 4.4 12.3 1.0
O A:VAL438 4.5 13.0 1.0
O A:PHE435 4.6 10.5 1.0
CA A:SER437 4.6 12.9 1.0
O A:HOH1948 4.7 32.1 1.0
C A:SER437 4.9 12.7 1.0

Reference:

A.C.Papageorgiou, J.Chen, D.Li. Crystal Structure and Biological Implications of A Glycoside Hydrolase Family 55 Beta-1,3-Glucanase From Chaetomium Thermophilum. Biochim. Biophys. Acta V.1865 1030 2017.
ISSN: ISSN 0006-3002
PubMed: 28479293
DOI: 10.1016/J.BBAPAP.2017.05.002
Page generated: Mon Oct 7 22:28:54 2024

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