Sodium in PDB 4bkr: Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh

All present enzymatic activity of Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh:
1.3.1.9;

The structure of Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh, PDB code: 4bkr was solved by M.W.Hirschbeck, C.Neckles, P.J.Tonge, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.580 / 1.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.590, 102.590, 84.990, 90.00, 90.00, 120.00
R / Rfree (%)	18.11 / 21.64

The binding sites of Sodium atom in the Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh (pdb code 4bkr). 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 Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh, PDB code: 4bkr:

Sodium binding site 1 out of 1 in the Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Enoyl-Acp Reductase From Yersinia Pestis (Wildtype, Removed Histag)with Cofactor Nadh within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1404 b:21.1 occ:1.00 OG A:SER138 3.0 10.8 0.9 O A:THR51 3.1 8.3 1.0 O5B A:NAI1400 3.1 12.1 1.0 N A:GLY54 3.1 9.2 1.0 O1N A:NAI1400 3.2 10.5 1.0 O A:SER138 3.3 12.3 1.0 O A:GLY48 3.4 11.4 1.0 C5D A:NAI1400 3.5 12.9 1.0 CA A:GLY54 3.7 9.4 1.0 C4B A:NAI1400 3.7 9.4 1.0 C5B A:NAI1400 3.7 12.2 1.0 N A:TYR53 3.7 8.6 1.0 PN A:NAI1400 3.8 9.8 1.0 O3 A:NAI1400 3.8 9.2 1.0 PA A:NAI1400 3.9 9.7 1.0 CB A:SER138 3.9 13.1 0.1 CB A:SER138 4.0 10.6 0.9 O1A A:NAI1400 4.1 9.3 1.0 C A:THR51 4.1 8.1 1.0 O5D A:NAI1400 4.1 11.3 1.0 C A:TYR53 4.1 9.2 1.0 C A:GLY52 4.2 8.3 1.0 CA A:TYR53 4.3 9.0 1.0 C A:SER138 4.3 15.8 1.0 CA A:GLY52 4.4 8.1 1.0 C A:GLY48 4.4 9.8 1.0 O3B A:NAI1400 4.5 11.2 1.0 C3B A:NAI1400 4.5 12.5 1.0 CB A:TYR53 4.6 9.8 1.0 N A:LEU55 4.6 8.8 1.0 OG1 A:THR51 4.6 11.9 1.0 C A:GLY54 4.7 9.2 1.0 N A:GLY52 4.7 8.0 1.0 O4B A:NAI1400 4.7 9.0 1.0 C4D A:NAI1400 4.8 9.5 1.0 CA A:SER138 4.8 14.3 0.1 CA A:SER138 4.8 14.3 0.9 CA A:GLY48 4.9 10.3 1.0 O A:GLY52 4.9 9.1 1.0 OG A:SER138 5.0 10.9 0.1

C.Neckles, M.W.Hirschbeck, S.Shah, P.Pan, G.R.Bommineni, W.Yu, N.Liu, S.Davoodi, C.Kisker, P.J.Tonge. Point Mutation Changes Substrate Binding Mechanism and Inhibitor Specificity of Yersinia Pestis Enoyl- Acp Reductase Fabv To Be Published.