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

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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

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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

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