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Sodium in PDB 4zju: Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad

Enzymatic activity of Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad

All present enzymatic activity of Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad:
1.3.1.9;

Protein crystallography data

The structure of Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad, PDB code: 4zju was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.92 / 1.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 71.020, 92.440, 93.830, 90.00, 90.00, 90.00
R / Rfree (%) 12.5 / 14.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad (pdb code 4zju). 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 Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad, PDB code: 4zju:

Sodium binding site 1 out of 1 in 4zju

Go back to Sodium Binding Sites List in 4zju
Sodium binding site 1 out of 1 in the Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:19.8
occ:0.86
O A:HOH677 2.3 14.2 0.5
O A:HOH657 2.4 31.9 1.0
O A:HOH442 2.5 20.9 0.4
O A:HOH581 2.5 13.5 1.0
O A:GLY104 2.6 13.0 1.0
OD1 A:ASN160 2.6 11.6 1.0
O A:HOH677 3.3 18.3 0.5
CG A:ASN160 3.4 10.1 1.0
ND2 A:ASN160 3.5 10.7 1.0
C A:GLY104 3.7 12.5 1.0
O A:HOH577 3.7 23.9 1.0
N A:PHE106 3.8 10.2 1.0
O A:HOH427 3.9 12.5 1.0
O A:HOH442 4.0 27.5 0.6
CA A:ASP105 4.1 11.7 1.0
N A:ASP105 4.3 12.2 1.0
C A:ASP105 4.3 10.8 1.0
O A:HOH466 4.5 19.0 1.0
CA A:PHE106 4.6 10.0 1.0
O A:HOH713 4.6 44.7 1.0
CB A:PHE106 4.6 9.8 1.0
CA A:GLY104 4.7 14.6 1.0
N A:GLY104 4.8 15.7 1.0
O A:HOH716 4.8 47.4 1.0
CB A:ASN160 4.9 9.5 1.0

Reference:

J.Abendroth, D.D.Lorimer, T.E.Edwards. Structure of A Nadh-Dependent Enoyl-Acp Reductase From Acinetobacter Baumannii in Complex with Nad To Be Published.
Page generated: Sun Aug 17 22:46:48 2025

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