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Zinc in PDB 3ugq: Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution

Enzymatic activity of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution

All present enzymatic activity of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution:
6.1.1.3;

Protein crystallography data

The structure of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution, PDB code: 3ugq was solved by K.M.Peterson, J.Ling, I.Simonovic, C.Cho, D.Soll, M.Simonovic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.46 / 2.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.970, 67.970, 191.367, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25

Other elements in 3ugq:

The structure of Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution also contains other interesting chemical elements:

Potassium (K) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution (pdb code 3ugq). 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 the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution, PDB code: 3ugq:

Zinc binding site 1 out of 1 in 3ugq

Go back to Zinc Binding Sites List in 3ugq
Zinc binding site 1 out of 1 in the Crystal Structure of the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution


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 the Apo Form of the Yeast Mitochondrial Threonyl- Trna Synthetase Determined at 2.1 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:24.9
occ:1.00
 NE2 A:HIS184 2.2 24.4 1.0
ND1 A:HIS319 2.2 20.2 1.0
SG A:CYS133 2.3 22.9 1.0
CD2 A:HIS184 3.1 23.6 1.0
CG A:HIS319 3.1 22.7 1.0
CE1 A:HIS184 3.2 25.7 1.0
CE1 A:HIS319 3.2 24.6 1.0
CB A:CYS133 3.3 22.6 1.0
CB A:HIS319 3.4 19.9 1.0
K A:K469 3.7 62.8 1.0
CA A:CYS133 3.9 23.6 1.0
OH A:TYR270 3.9 21.6 1.0
N A:CYS133 4.0 23.3 1.0
CD2 A:HIS319 4.2 19.6 1.0
ND1 A:HIS184 4.2 23.2 1.0
CG A:HIS184 4.2 23.2 1.0
NE2 A:HIS319 4.2 24.2 1.0
SD A:MET131 4.3 37.4 1.0
OD1 A:ASP182 4.4 38.6 1.0
CA A:HIS319 4.4 19.9 1.0
OE1 A:GLN292 4.5 25.9 1.0
CZ A:TYR270 4.7 23.6 1.0
CG A:MET131 4.8 26.6 1.0
CB A:MET131 4.8 30.1 1.0

Reference:

J.Ling, K.M.Peterson, I.Simonovic, C.Cho, D.Soll, M.Simonovic. Yeast Mitochondrial Threonyl-Trna Synthetase Recognizes Trna Isoacceptors By Distinct Mechanisms and Promotes Cun Codon Reassignment. Proc.Natl.Acad.Sci.Usa V. 109 3281 2012.
ISSN: ISSN 0027-8424
PubMed: 22343532
DOI: 10.1073/PNAS.1200109109
Page generated: Sat Oct 26 17:18:44 2024

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