Potassium in PDB 7r2w: Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine

Enzymatic activity of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine

All present enzymatic activity of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine:
2.5.1.6;

Protein crystallography data

The structure of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine, PDB code: 7r2w was solved by A.Shahar, D.Kleiner, S.Bershtein, R.Zarivach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	62.73 / 1.60
*Space group*	P 4₂ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	86.611, 86.611, 90.982, 90, 90, 90
*R / R_free (%)*	18.2 / 22

Other elements in 7r2w:

The structure of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine (pdb code 7r2w). 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 Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine, PDB code: 7r2w:

Potassium binding site 1 out of 1 in 7r2w

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Potassium Binding Sites List in 7r2w

Potassium binding site 1 out of 1 in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K404 b:44.5 occ:1.00	O2B	A:ANP401	3.0	30.4	0.5
	O	A:CYS240	3.0	31.9	1.0
	OD1	A:ASP239	3.0	63.0	1.0
	O	A:HOH543	3.2	37.0	1.0
	O	A:HOH541	3.5	42.0	1.0
	CB	A:CYS240	3.8	33.2	0.5
	CG	A:ASP239	3.9	54.4	1.0
	C	A:CYS240	3.9	28.4	1.0
	N	A:CYS240	3.9	30.1	1.0
	CB	A:CYS240	4.0	27.0	0.5
	CA	A:CYS240	4.1	30.4	0.5
	CA	A:CYS240	4.2	27.7	0.5
	MG	A:MG403	4.2	46.3	1.0
	OD2	A:ASP239	4.3	62.1	1.0
	PB	A:ANP401	4.3	37.0	0.5
	NH2	A:ARG245	4.6	27.2	1.0
	C	A:ASP239	4.6	38.8	1.0
	O1B	A:ANP401	4.8	35.7	0.5
	SG	A:CYS240	4.8	37.5	0.5
	CD1	A:LEU242	4.9	37.0	1.0
	CA	A:ASP239	4.9	39.7	1.0
	CB	A:ASP239	5.0	43.9	1.0

Reference:

D.Kleiner, Z.Shapiro Tuchman, F.Shmulevich, A.Shahar, R.Zarivach, M.Kosloff, S.Bershtein. Evolution of Homo-Oligomerization of Methionine S-Adenosyltransferases Is Replete with Structure-Function Constrains. Protein Sci. V. 31 E4352 2022.
ISSN: ESSN 1469-896X
PubMed: 35762725
DOI: 10.1002/PRO.4352

Page generated: Wed Apr 5 10:09:11 2023

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