Chlorine in PDB 9deu: Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine

Enzymatic activity of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine

All present enzymatic activity of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine:
1.17.99.6;

Protein crystallography data

The structure of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine, PDB code: 9deu was solved by Y.Hu, S.D.Bruner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	36.90 / 1.70
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	53.647, 105.194, 73.792, 90, 90, 90
*R / R_free (%)*	21.9 / 22.9

Other elements in 9deu:

The structure of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Zinc	(Zn)	1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine (pdb code 9deu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine, PDB code: 9deu:

Chlorine binding site 1 out of 1 in 9deu

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Chlorine Binding Sites List in 9deu

Chlorine binding site 1 out of 1 in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl203 b:41.5 occ:1.00	ZN	A:ZN204	2.2	29.3	1.0
	O12	A:56B201	2.5	67.7	1.0
	O	A:HOH304	3.3	56.3	1.0
	OD2	A:ASP13	3.4	29.4	1.0
	SG	A:CYS9	3.6	25.9	1.0
	O11	A:56B201	3.7	74.0	1.0
	SG	A:CYS10	3.8	28.2	1.0
	O	A:HOH312	3.8	38.1	1.0
	C12	A:56B201	3.8	72.5	1.0
	NE2	A:GLN166	3.8	53.4	1.0
	CB	A:CYS9	3.8	22.6	1.0
	NZ	A:LYS120	4.2	59.2	1.0
	C11	A:56B201	4.3	75.3	1.0
	CB	A:CYS10	4.4	28.5	1.0
	CD2	A:LEU114	4.5	30.5	1.0
	C13	A:56B201	4.6	77.8	1.0
	OG	A:SER117	4.6	50.7	1.0
	O	A:CYS169	4.7	67.0	1.0
	CG	A:ASP13	4.7	29.0	1.0
	C	A:CYS9	4.7	25.6	1.0
	O	A:CYS9	4.9	26.0	1.0
	CA	A:CYS9	4.9	24.1	1.0
	N	A:CYS10	4.9	23.9	1.0

Reference:

Y.Hu, M.Jaroch, G.Sun, P.C.Dedon, V.De Crecy-Lagard, S.D.Bruner. Mechanism of Catalysis and Substrate Binding of Epoxyqueuosine Reductase in the Biosynthetic Pathway to Queuosine-Modified Trna. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 39644232
DOI: 10.1021/ACS.BIOCHEM.4C00524

Page generated: Sat Feb 8 17:30:48 2025

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