Sodium in PDB 6xnc: Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate

Enzymatic activity of Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate

All present enzymatic activity of Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate:
4.2.1.20;

Protein crystallography data

The structure of Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate, PDB code: 6xnc was solved by R.S.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	34.52 / 2.11
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	182.289, 57.529, 67.266, 90, 94.83, 90
*R / R_free (%)*	16.3 / 21.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate (pdb code 6xnc). 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 Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate, PDB code: 6xnc:

Sodium binding site 1 out of 1 in 6xnc

Go back to

Sodium Binding Sites List in 6xnc

Sodium binding site 1 out of 1 in the Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Salmonella Typhimurium Tryptophan Synthase Complexed with L-Tryptophan and D-Glycerol-3-Phosphate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Na401 b:24.4 occ:1.00	O	B:HOH533	2.4	29.6	1.0
	O	B:SER308	2.4	22.8	1.0
	O	B:GLY232	2.5	19.6	1.0
	O	B:HOH597	2.5	16.0	1.0
	O	B:PHE306	2.7	27.4	1.0
	C	B:GLY232	3.5	19.6	1.0
	C	B:SER308	3.6	21.2	1.0
	C	B:PHE306	3.7	31.3	1.0
	CD	B:PRO270	3.8	26.1	1.0
	CG	B:PRO270	3.9	24.0	1.0
	O	B:GLY268	3.9	20.4	1.0
	CB	B:PHE306	4.0	26.8	1.0
	N	B:SER308	4.1	29.4	1.0
	CA	B:GLY232	4.1	17.1	1.0
	CD2	B:PHE306	4.1	26.8	1.0
	CA	B:PHE306	4.3	30.4	1.0
	O	B:LEU304	4.4	26.9	1.0
	CA	B:SER308	4.4	27.8	1.0
	N	B:PHE306	4.4	32.8	1.0
	O	B:VAL231	4.5	21.4	1.0
	CG	B:PHE306	4.5	32.4	1.0
	N	B:VAL309	4.5	23.8	1.0
	CB	B:VAL309	4.6	21.3	1.0
	CA	B:VAL309	4.6	19.9	1.0
	C	B:PRO307	4.7	31.0	1.0
	N	B:GLY233	4.7	21.6	1.0
	N	B:PRO307	4.7	31.6	1.0
	C	B:GLY268	4.8	18.5	1.0
	OE2	B:GLU256	4.9	23.9	1.0

Reference:

R.S.Phillips, A.P.Harris. Structural Basis of the Stereochemistry of Inhibition of Tryptophan Synthase By Tryptophan and Derivatives. Biochemistry V. 60 231 2021.
ISSN: ISSN 0006-2960
PubMed: 33428374
DOI: 10.1021/ACS.BIOCHEM.0C00635

Page generated: Tue Oct 8 14:52:18 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy