Potassium in PDB 8eh1: Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline

Enzymatic activity of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline

All present enzymatic activity of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline:
4.2.1.20;

Protein crystallography data

The structure of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline, PDB code: 8eh1 was solved by N.J.Porter, P.J.Almhjell, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.86 / 2.00
*Space group*	I 4
*Cell size a, b, c (Å), α, β, γ (°)*	164.862, 164.862, 84.057, 90, 90, 90
*R / R_free (%)*	18.8 / 21.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline (pdb code 8eh1). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline, PDB code: 8eh1:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 8eh1

Go back to

Potassium Binding Sites List in 8eh1

Potassium binding site 1 out of 2 in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K403 b:36.8 occ:1.00	O	A:TYR301	2.6	31.1	1.0
	O	A:GLY303	2.7	28.3	1.0
	O	A:HOH502	2.8	37.9	1.0
	OG	A:SER265	2.8	31.4	1.0
	O	A:ALA263	2.9	29.1	1.0
	C	A:GLY303	3.7	36.0	1.0
	O	A:SER228	3.7	35.9	1.0
	C	A:TYR301	3.7	37.4	1.0
	CB	A:SER265	3.8	28.1	1.0
	O	A:HOH552	3.8	34.9	1.0
	OG	A:SER228	3.8	67.7	1.0
	C	A:ALA263	4.0	33.6	1.0
	N	A:GLY303	4.0	31.5	1.0
	C	A:SER228	4.1	30.7	1.0
	CA	A:SER228	4.1	39.7	1.0
	N	A:SER265	4.1	33.6	1.0
	C	A:PRO302	4.2	33.5	1.0
	CB	A:ALA263	4.3	31.9	1.0
	CA	A:GLY303	4.4	29.3	1.0
	CA	A:PRO302	4.5	26.6	1.0
	N	A:PRO302	4.5	32.2	1.0
	CB	A:SER228	4.6	50.1	1.0
	O	A:LEU299	4.6	33.5	1.0
	CB	A:TYR301	4.6	28.6	1.0
	CA	A:SER265	4.6	31.7	1.0
	CA	A:ALA263	4.6	28.9	1.0
	CA	A:TYR301	4.6	31.1	1.0
	O	A:PRO302	4.6	32.5	1.0
	N	A:VAL304	4.7	30.9	1.0
	CD2	A:TYR301	4.7	34.5	1.0
	OE2	A:GLU251	4.7	38.6	1.0
	N	A:TYR301	4.9	33.9	1.0
	CB	A:VAL304	4.9	28.9	1.0
	CA	A:VAL304	4.9	29.1	1.0
	N	A:ALA264	5.0	28.1	1.0
	N	A:GLY229	5.0	31.6	1.0

Potassium binding site 2 out of 2 in 8eh1

Go back to

Potassium Binding Sites List in 8eh1

Potassium binding site 2 out of 2 in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate and Complexed with 4-Hydroxyquinoline within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:K403 b:39.5 occ:1.00	O	B:HOH501	2.6	41.6	1.0
	O	B:GLY303	2.6	33.2	1.0
	O	B:TYR301	2.6	33.1	1.0
	O	B:ALA263	2.8	32.0	1.0
	OG	B:SER265	2.8	42.7	1.0
	O	B:SER228	3.7	42.6	1.0
	OG	B:SER228	3.7	62.7	1.0
	C	B:GLY303	3.7	34.6	1.0
	C	B:TYR301	3.8	36.3	1.0
	CB	B:SER265	3.8	35.8	1.0
	O	B:HOH524	3.8	37.7	1.0
	C	B:ALA263	3.9	40.7	1.0
	N	B:GLY303	4.0	32.5	1.0
	C	B:SER228	4.0	41.3	1.0
	CA	B:SER228	4.1	48.3	1.0
	N	B:SER265	4.1	40.7	1.0
	CB	B:ALA263	4.2	39.0	1.0
	C	B:PRO302	4.2	44.8	1.0
	OE2	B:GLU251	4.4	54.1	1.0
	CA	B:GLY303	4.4	26.8	1.0
	CB	B:SER228	4.5	49.1	1.0
	CA	B:ALA263	4.5	37.1	1.0
	N	B:PRO302	4.6	38.2	1.0
	CA	B:PRO302	4.6	34.2	1.0
	O	B:LEU299	4.6	41.8	1.0
	CA	B:SER265	4.6	39.9	1.0
	CD2	B:TYR301	4.6	35.2	1.0
	CB	B:TYR301	4.6	32.7	1.0
	CA	B:TYR301	4.7	32.5	1.0
	N	B:VAL304	4.7	34.3	1.0
	O	B:PRO302	4.7	35.4	1.0
	N	B:TYR301	4.9	40.6	1.0
	CB	B:VAL304	4.9	32.4	1.0
	N	B:ALA264	4.9	35.6	1.0
	N	B:GLY229	4.9	36.1	1.0
	CA	B:VAL304	5.0	29.1	1.0

Reference:

N.J.Porter, P.J.Almhjell, F.H.Arnold. Noncanonical L-Tyrosine Synthesis By Evolved Tryptophan Synthases To Be Published.

Page generated: Mon Aug 12 23:35:40 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

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