Sodium in PDB 7txq: X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea

The structure of X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea, PDB code: 7txq was solved by N.R.Herkert, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.46 / 1.65
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	97.413, 97.413, 72.842, 90, 90, 120
R / Rfree (%)	17.2 / 20.4

The binding sites of Sodium atom in the X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea (pdb code 7txq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea, PDB code: 7txq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea within 5.0Å range: probe atom residue distance (Å) B Occ A:Na303 b:8.4 occ:0.33 O A:HOH434 2.4 17.6 1.0 OD1 A:ASN130 2.4 17.6 1.0 CG A:ASN130 3.4 14.1 1.0 ND2 A:ASN130 3.7 16.9 1.0 O A:HOH574 4.3 18.4 1.0 O A:GLY112 4.6 10.3 1.0 CB A:ASN130 4.8 11.2 1.0

Sodium binding site 2 out of 2 in the X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of X-Ray Structure of the Viob N-Acetyltransferase From Acinetobacter Baumannii in the Present of Tdp and Acetyl-Coenzymea within 5.0Å range: probe atom residue distance (Å) B Occ A:Na304 b:3.6 occ:0.33 OD1 A:ASN166 2.3 8.1 1.0 O A:HOH448 2.3 9.7 1.0 CG A:ASN166 3.3 7.3 1.0 ND2 A:ASN166 3.6 7.3 1.0 O A:ASN148 4.3 6.5 1.0 O A:HOH487 4.3 15.2 1.0 CB A:ASN148 4.5 6.8 1.0 CB A:ASN166 4.7 7.3 1.0

N.R.Herkert, J.B.Thoden, H.M.Holden. Structure and Function of An N-Acetyltransferase From the Human Pathogen Acinetobacter Baumannii Isolate BAL_212. Proteins V. 90 1594 2022.
ISSN: ESSN 1097-0134
PubMed: 35277885
DOI: 10.1002/PROT.26334