Potassium in PDB 5t5m: Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A.

Enzymatic activity of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A.

All present enzymatic activity of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A.:
1.2.99.5;

Protein crystallography data

The structure of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A., PDB code: 5t5m was solved by T.Wagner, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.22 / 2.50
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	105.543, 105.543, 340.549, 90.00, 90.00, 120.00
*R / R_free (%)*	15.8 / 18.2

Other elements in 5t5m:

The structure of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A. also contains other interesting chemical elements:

Tungsten	(W)	1 atom
Magnesium	(Mg)	3 atoms
Zinc	(Zn)	2 atoms
Iron	(Fe)	44 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A. (pdb code 5t5m). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A., PDB code: 5t5m:

Potassium binding site 1 out of 1 in 5t5m

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Potassium Binding Sites List in 5t5m

Potassium binding site 1 out of 1 in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A.

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Trigonal Form at 2.5 A. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:K501 b:0.7 occ:1.00	O	D:GLU18	2.6	85.2	1.0
	O	B:VAL43	2.8	82.7	1.0
	O	B:SER40	3.2	80.8	1.0
	CA	B:HIS44	3.7	91.3	1.0
	C	B:VAL43	3.7	82.2	1.0
	C	D:GLU18	3.8	82.8	1.0
	O	D:SER19	3.9	78.2	1.0
	N	B:ALA45	4.0	83.2	1.0
	CA	D:SER19	4.0	78.5	1.0
	N	B:HIS44	4.1	88.4	1.0
	O	B:LYS41	4.1	67.7	1.0
	C	B:HIS44	4.3	88.5	1.0
	C	B:SER40	4.3	73.8	1.0
	C	D:SER19	4.3	79.5	1.0
	N	D:SER19	4.3	78.4	1.0
	CA	B:LYS41	4.5	64.6	1.0
	C	B:LYS41	4.6	66.8	1.0
	NE2	B:HIS368	4.7	0.0	1.0
	CE1	B:HIS368	4.7	0.1	1.0
	CB	B:HIS44	4.8	95.9	1.0
	ND1	B:HIS44	4.9	0.5	1.0
	N	B:VAL43	4.9	75.4	1.0
	N	B:LYS41	4.9	65.5	1.0
	CB	B:ALA45	5.0	80.6	1.0
	CA	B:VAL43	5.0	78.7	1.0
	CA	D:GLU18	5.0	82.2	1.0

Reference:

T.Wagner, U.Ermler, S.Shima. The Methanogenic CO2 Reducing-and-Fixing Enzyme Is Bifunctional and Contains 46 [4FE-4S] Clusters. Science V. 354 114 2016.
ISSN: ESSN 1095-9203
PubMed: 27846502
DOI: 10.1126/SCIENCE.AAF9284

Page generated: Mon Aug 12 14:32:48 2024

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