Sodium in PDB 4mkj: Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine

Enzymatic activity of Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine

All present enzymatic activity of Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine:
4.4.1.11;

Protein crystallography data

The structure of Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine, PDB code: 4mkj was solved by S.V.Revtovich, A.D.Nikulin, E.A.Morozova, L.N.Zakomirdina, T.V.Demidkina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.07 / 1.85
*Space group*	I 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	56.440, 122.670, 128.280, 90.00, 90.00, 90.00
*R / R_free (%)*	15.5 / 19.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine (pdb code 4mkj). 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 Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine, PDB code: 4mkj:

Sodium binding site 1 out of 1 in 4mkj

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Sodium Binding Sites List in 4mkj

Sodium binding site 1 out of 1 in the Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na404 b:33.9 occ:1.00	OH	A:TYR154	2.5	19.0	1.0
	OE1	A:GLU156	2.6	31.9	1.0
	OD2	A:ASP185	2.7	21.1	1.0
	OG1	A:THR116	3.1	30.3	1.0
	CZ	A:TYR154	3.4	14.6	1.0
	CD	A:GLU156	3.5	32.1	1.0
	CE2	A:TYR154	3.6	18.1	1.0
	CG	A:ASP185	3.6	19.4	1.0
	CB	A:ASP185	3.7	14.4	1.0
	CB	A:THR116	3.7	28.9	1.0
	CG2	A:THR116	3.7	24.5	1.0
	CD1	A:ILE92	3.8	20.1	1.0
	CG	A:GLU156	3.8	33.7	1.0
	N1	A:LLP210	3.9	27.3	1.0
	CB	A:TYR113	4.0	34.5	1.0
	N	A:TYR113	4.3	30.3	1.0
	OE2	A:GLU156	4.5	29.5	1.0
	C6	A:LLP210	4.5	30.7	1.0
	CB	A:ILE112	4.6	28.2	1.0
	CE1	A:TYR154	4.7	19.1	1.0
	CB	A:GLU156	4.7	27.2	1.0
	OD1	A:ASP185	4.7	17.3	1.0
	C2'	A:LLP210	4.8	25.7	1.0
	CG1	A:ILE92	4.8	17.6	1.0
	C2	A:LLP210	4.8	28.4	1.0
	CA	A:TYR113	4.8	33.4	1.0
	CD2	A:TYR154	4.9	17.0	1.0
	CG2	A:ILE112	5.0	30.4	1.0

Reference:

E.A.Morozova, S.V.Revtovich, N.V.Anufrieva, V.V.Kulikova, A.D.Nikulin, T.V.Demidkina. Alliin Is A Suicide Substrate of Citrobacter Freundii Methionine [Gamma]-Lyase: Structural Bases of Inactivation of the Enzyme Acta Crystallogr.,Sect.D V. 70 3034 2014.
ISSN: ISSN 0907-4449
DOI: 10.1107/S1399004714020938

Page generated: Mon Oct 7 17:00:22 2024

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