Sodium in PDB 4euh: Crystal Structure of Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form

The structure of Crystal Structure of Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form, PDB code: 4euh was solved by K.Hu, M.Zhao, T.Zhang, S.Yang, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.054, 77.588, 107.224, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 23.4

The binding sites of Sodium atom in the Crystal Structure of Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form (pdb code 4euh). 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 Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form, PDB code: 4euh:

Sodium binding site 1 out of 1 in the Crystal Structure of Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form


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 Clostridium Acetobutulicum Trans-2-Enoyl-Coa Reductase Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Na401 b:37.6 occ:1.00 O A:SER138 2.8 32.1 1.0 O A:SER50 2.9 28.2 1.0 O A:GLY47 2.9 26.7 1.0 N A:GLY53 3.0 25.6 1.0 O A:HOH673 3.3 44.1 1.0 OG A:SER138 3.4 30.1 1.0 CA A:GLY53 3.6 25.1 1.0 CB A:SER138 3.6 30.2 1.0 N A:PHE52 3.7 26.5 1.0 C A:SER138 3.9 31.5 1.0 C A:SER50 4.0 28.2 1.0 C A:PHE52 4.0 26.0 1.0 C A:GLY47 4.1 26.2 1.0 C A:GLY51 4.2 26.7 1.0 CA A:PHE52 4.2 26.6 1.0 CA A:SER138 4.4 30.1 1.0 CB A:PHE52 4.5 27.0 1.0 CA A:GLY51 4.5 27.0 1.0 CA A:GLY47 4.6 26.2 1.0 N A:GLY51 4.7 27.6 1.0 C A:GLY53 4.7 24.6 1.0 N A:LEU54 4.7 24.4 1.0 O A:GLY51 4.9 26.3 1.0 N A:SER50 4.9 28.3 1.0 OG A:SER50 4.9 30.1 1.0

K.Hu, M.Zhao, T.Zhang, M.Zha, C.Zhong, Y.Jiang, J.Ding. Structures of Trans-2-Enoyl-Coa Reductases From Clostridium Acetobutylicum and Treponema Denticola: Insights Into the Substrate Specificity and the Catalytic Mechanism Biochem.J. V. 449 79 2013.
ISSN: ISSN 0264-6021
PubMed: 23050861
DOI: 10.1042/BJ20120871