Sodium in PDB 2vu1: Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate.

All present enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate.:
2.3.1.9;

The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate., PDB code: 2vu1 was solved by P.Kursula, W.Schmitz, R.K.Wierenga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.51
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	84.298, 78.737, 148.339, 90.00, 92.93, 90.00
R / Rfree (%)	21.5 / 24.7

The binding sites of Sodium atom in the Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate. (pdb code 2vu1). 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 Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate., PDB code: 2vu1:

Sodium binding site 1 out of 1 in the Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Biosynthetic Thiolase From Z. Ramigera. Complex of with O-Pantheteine- 11-Pivalate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1394 b:57.3 occ:1.00 O A:HOH2042 2.3 10.5 1.0 OE1 A:GLU29 2.7 23.0 1.0 CD A:GLU29 3.6 21.4 1.0 OE2 A:GLU29 3.7 28.6 1.0 O A:ASN24 3.8 12.0 1.0 O A:HOH2244 3.8 13.2 1.0 CD A:PRO26 4.0 9.8 1.0 O A:HOH2051 4.0 20.7 1.0 CA A:THR25 4.2 10.2 1.0 OG1 A:THR25 4.3 10.2 1.0 CB A:THR25 4.6 9.8 1.0 C A:ASN24 4.7 9.2 1.0 CG2 A:THR25 4.7 6.4 1.0 N A:THR25 4.9 9.2 1.0 O A:LYS205 5.0 22.9 1.0 CG A:PRO26 5.0 10.2 1.0 CG A:GLU29 5.0 11.4 1.0

G.Merilainen, W.Schmitz, R.K.Wierenga, P.Kursula. The Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine Are Required For A Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, A Thioester-Dependent Enzyme. Febs J. V. 275 6136 2008.
ISSN: ISSN 1742-464X
PubMed: 19016856
DOI: 10.1111/J.1742-4658.2008.06737.X