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 / R_free (%)*	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

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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 Dec 15 12:21:54 2020

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