Atomistry » Sodium » PDB 2vrr-2wcp » 2vu1
Atomistry »
  Sodium »
    PDB 2vrr-2wcp »
      2vu1 »

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

Enzymatic activity of 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;

Protein crystallography data

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

Sodium Binding Sites:

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 2vu1

Go back to Sodium Binding Sites List in 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

Reference:

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
Page generated: Tue Dec 15 05:56:47 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy