Sodium in PDB 2vjp: Formyl-Coa Transferase Mutant Variant W48F

All present enzymatic activity of Formyl-Coa Transferase Mutant Variant W48F:
2.8.3.16;

The structure of Formyl-Coa Transferase Mutant Variant W48F, PDB code: 2vjp was solved by C.G.Toyota, C.L.Berthold, A.Gruez, S.Jonsson, Y.Lindqvist, C.Cambillau, N.G.J.Richards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.95
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	152.716, 152.716, 99.448, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 20.1

The binding sites of Sodium atom in the Formyl-Coa Transferase Mutant Variant W48F (pdb code 2vjp). 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 Formyl-Coa Transferase Mutant Variant W48F, PDB code: 2vjp:

Sodium binding site 1 out of 1 in the Formyl-Coa Transferase Mutant Variant W48F


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Formyl-Coa Transferase Mutant Variant W48F within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1429 b:23.7 occ:1.00 O A:ASP294 2.4 12.5 1.0 O A:HOH2344 2.5 24.2 1.0 OD1 A:ASP297 2.6 17.8 0.5 C A:ASP294 3.5 12.5 1.0 CG A:ASP297 3.6 15.4 0.5 O A:HOH2340 4.0 39.2 1.0 CA A:ASP294 4.2 13.1 1.0 OD2 A:ASP297 4.2 16.9 0.5 OD1 A:ASP297 4.3 14.3 0.5 OH A:TYR343 4.3 14.6 1.0 CA A:ASP297 4.4 14.1 0.5 CA A:ASP297 4.4 14.3 0.5 N A:ASP297 4.4 13.9 1.0 CB A:ASP297 4.5 14.2 0.5 N A:MET295 4.5 12.1 1.0 O A:MET295 4.6 12.4 1.0 CB A:ASP297 4.6 14.6 0.5 CB A:ASP294 4.7 13.5 1.0 C A:MET295 4.7 12.2 1.0 CG A:ASP297 4.7 14.3 0.5 CA A:MET295 4.7 12.3 1.0

C.G.Toyota, C.L.Berthold, A.Gruez, S.Jonsson, Y.Lindqvist, C.Cambillau, N.G.J.Richards. Differential Substrate Specificity and Kinetic Behavior of Escherichia Coli Yfdw and Oxalobacter Formigenes Formyl Coenzyme A Transferase. J.Bacteriol. V. 190 2556 2008.
ISSN: ISSN 0021-9193
PubMed: 18245280
DOI: 10.1128/JB.01823-07