Sodium in PDB 5a8w: Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution, PDB code: 5a8w was solved by T.Wagner, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.66 / 1.80
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	110.391, 102.185, 118.739, 89.20, 93.97, 90.98
*R / R_free (%)*	16.5 / 20.1

Other elements in 5a8w:

The structure of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution also contains other interesting chemical elements:

Nickel

(Ni)

4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution (pdb code 5a8w). 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 Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution, PDB code: 5a8w:

Sodium binding site 1 out of 1 in 5a8w

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Sodium Binding Sites List in 5a8w

Sodium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
F:Na1270 b:37.0 occ:1.00	OD2	F:ASP229	2.2	40.6	1.0
	N	F:ALA226	2.9	18.7	1.0
	CG	F:ASP229	3.2	33.5	1.0
	CA	F:ILE225	3.4	13.4	1.0
	C	F:ILE225	3.6	16.1	1.0
	CB	F:ALA226	3.7	20.3	1.0
	O	F:ASN224	3.8	17.4	1.0
	CA	F:ALA226	3.9	15.2	1.0
	CB	F:ASP229	3.9	20.7	1.0
	OD1	F:ASP229	4.1	34.9	1.0
	CG2	F:ILE225	4.2	11.1	1.0
	CB	F:ILE225	4.3	11.6	1.0
	N	F:ILE225	4.4	13.7	1.0
	C	F:ASN224	4.5	14.7	1.0
	O	F:ALA226	4.5	11.3	1.0
	O	F:LYS222	4.5	16.5	1.0
	C	F:ALA226	4.7	14.0	1.0
	O	F:ILE225	4.8	12.8	1.0
	CG1	F:ILE225	4.9	10.2	1.0

Reference:

T.Wagner, J.Kahnt, U.Ermler, S.Shima. Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation. Angew.Chem.Int.Ed.Engl. V. 55 10630 2016.
ISSN: ISSN 1433-7851
PubMed: 27467699
DOI: 10.1002/ANIE.201603882

Page generated: Tue Dec 15 10:11:33 2020

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