Sodium in PDB 4o1q: Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q was solved by E.T.Yukl, C.W.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	44.49 / 2.59
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	55.530, 83.520, 107.780, 109.94, 91.54, 105.78
*R / R_free (%)*	19.8 / 25.4

Other elements in 4o1q:

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Calcium	(Ca)	2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 4o1q). 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 the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q:

Sodium binding site 1 out of 1 in 4o1q

Go back to

Sodium Binding Sites List in 4o1q

Sodium binding site 1 out of 1 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

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 the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
F:Na402 b:52.9 occ:1.00	OG	F:SER256	2.6	57.3	1.0
	O	F:ASP258	2.6	54.4	1.0
	O	F:ASP253	2.8	51.3	1.0
	OD2	F:ASP253	2.9	54.7	1.0
	C	F:ASP253	3.4	51.1	1.0
	N	F:SER256	3.4	55.3	1.0
	CB	F:SER256	3.4	57.9	1.0
	CG	F:ASP253	3.5	53.3	1.0
	N	F:SER255	3.7	52.0	1.0
	CG	F:LYS260	3.8	58.5	1.0
	C	F:ASP258	3.8	54.7	1.0
	N	F:LEU254	3.9	50.5	1.0
	CA	F:LEU254	3.9	50.4	1.0
	C	F:LEU254	3.9	51.0	1.0
	N	F:LYS260	3.9	54.9	1.0
	CA	F:SER256	4.0	56.7	1.0
	CB	F:ASP253	4.1	52.8	1.0
	CB	F:LYS260	4.1	58.0	1.0
	OD1	F:ASP253	4.2	52.5	1.0
	OG	F:SER255	4.3	54.3	1.0
	CA	F:ASP253	4.4	51.2	1.0
	C	F:SER255	4.5	54.2	1.0
	N	F:ASP258	4.5	55.7	1.0
	CA	F:SER255	4.6	52.8	1.0
	CA	F:LYS260	4.6	56.2	1.0
	C	F:ALA259	4.6	54.5	1.0
	O	F:LEU254	4.6	51.0	1.0
	N	F:ALA259	4.7	53.8	1.0
	CA	F:ALA259	4.8	53.2	1.0
	CA	F:ASP258	4.8	55.5	1.0
	C	F:SER256	4.8	56.5	1.0
	N	F:GLY257	4.9	55.2	1.0

Reference:

S.Shin, E.T.Yukl, E.Sehanobish, C.M.Wilmot, V.L.Davidson. Site-Directed Mutagenesis of GLN103 Reveals the Influence of This Residue on the Redox Properties and Stability of Maug. Biochemistry V. 53 1342 2014.
ISSN: ISSN 0006-2960
PubMed: 24517455
DOI: 10.1021/BI5000349

Page generated: Mon Oct 7 17:22:45 2024

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