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Sodium in PDB 6hr7: Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution

Enzymatic activity of Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution

All present enzymatic activity of Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution:
1.1.1.34;

Protein crystallography data

The structure of Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution, PDB code: 6hr7 was solved by T.Wagner, B.Voegeli, T.J.Erb, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.61 / 2.40
Space group P 31 1 2
Cell size a, b, c (Å), α, β, γ (°) 83.322, 83.322, 211.212, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 22

Other elements in 6hr7:

The structure of Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution (pdb code 6hr7). 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 Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution, PDB code: 6hr7:

Sodium binding site 1 out of 1 in 6hr7

Go back to Sodium Binding Sites List in 6hr7
Sodium binding site 1 out of 1 in the Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Hmg-Coa Reductase From Methanothermococcus Thermolithotrophicus Apo Form at 2.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:0.8
occ:1.00
OE2 A:GLU59 2.8 98.2 1.0
CG A:ARG351 3.6 80.6 1.0
NE A:ARG351 3.6 87.4 1.0
CD A:GLU59 3.7 97.9 1.0
CD A:ARG351 4.0 81.2 1.0
OE1 A:GLU59 4.1 0.2 1.0
CZ A:ARG351 4.4 89.5 1.0
NH1 A:ARG351 4.6 91.4 1.0
CG A:GLU59 4.8 95.5 1.0
CB A:ARG351 4.9 64.3 1.0
O A:ARG351 4.9 67.5 1.0

Reference:

B.Vogeli, S.Shima, T.J.Erb, T.Wagner. Crystal Structure of Archaeal Hmg-Coa Reductase: Insights Into Structural Changes of the C-Terminal Helix of the Class-I Enzyme. Febs Lett. V. 593 543 2019.
ISSN: ISSN 0014-5793
PubMed: 30702149
DOI: 10.1002/1873-3468.13331
Page generated: Tue Oct 8 09:23:38 2024

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