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Zinc 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 / Rfree (%) 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
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Epoxyqueuosine Reductase Queh in Complex with Queuosine, PDB code: 9deu:

Zinc binding site 1 out of 1 in 9deu

Go back to Zinc Binding Sites List in 9deu
Zinc 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 Zinc with other atoms in the Zn 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:Zn204

b:29.3
occ:1.00
 OD2 A:ASP13 2.0 29.4 1.0
SG A:CYS9 2.2 25.9 1.0
CL A:CL203 2.2 41.5 1.0
SG A:CYS10 2.3 28.2 1.0
CG A:ASP13 2.9 29.0 1.0
CB A:CYS9 3.3 22.6 1.0
CB A:CYS10 3.4 28.5 1.0
CB A:ASP13 3.4 22.1 1.0
N A:CYS10 3.6 23.9 1.0
C A:CYS9 3.9 25.6 1.0
CA A:CYS10 4.0 22.7 1.0
OD1 A:ASP13 4.0 31.6 1.0
CA A:CYS9 4.1 24.1 1.0
O12 A:56B201 4.2 67.7 1.0
NE2 A:GLN166 4.3 53.4 1.0
O A:CYS10 4.5 22.7 1.0
O11 A:56B201 4.5 74.0 1.0
O A:CYS9 4.5 26.0 1.0
N A:ASP13 4.6 23.1 1.0
CA A:ASP13 4.6 22.1 1.0
C A:CYS10 4.6 23.2 1.0
O A:HOH312 4.7 38.1 1.0
OG A:SER117 4.8 50.7 1.0
N A:CYS9 4.8 22.2 1.0
OG1 A:THR113 4.9 21.1 1.0
CD2 A:LEU114 4.9 30.5 1.0
CB A:SER117 4.9 40.1 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: Sun Feb 9 01:02:05 2025

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