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Zinc in PDB 6iy6: Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs)

Enzymatic activity of Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs)

All present enzymatic activity of Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs):
6.1.1.12; 6.1.1.15; 6.1.1.17;

Protein crystallography data

The structure of Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs), PDB code: 6iy6 was solved by S.H.Park, H.Hahn, B.W.Han, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.60
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 108.068, 108.068, 815.642, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 27.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs) (pdb code 6iy6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs), PDB code: 6iy6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6iy6

Go back to Zinc Binding Sites List in 6iy6
Zinc binding site 1 out of 2 in the Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs)


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 Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:0.4
occ:1.00
 ND1 A:HIS204 3.5 0.4 1.0
ND1 B:HIS204 3.5 0.8 1.0
OE1 A:GLU208 3.6 0.2 1.0
OE1 B:GLU208 3.7 0.2 1.0
CE1 A:HIS204 3.8 0.6 1.0
CE1 B:HIS204 3.8 0.5 1.0
CB B:ARG207 3.9 0.4 1.0
CB A:ARG207 4.0 0.5 1.0
CD B:ARG207 4.2 1.0 1.0
CD A:ARG207 4.2 0.9 1.0
N B:GLU208 4.5 0.3 1.0
N A:GLU208 4.5 0.0 1.0
O B:HIS204 4.5 0.1 1.0
O A:HIS204 4.5 0.4 1.0
CG B:ARG207 4.7 0.5 1.0
CG A:HIS204 4.7 0.2 1.0
CG A:ARG207 4.7 0.0 1.0
CG B:HIS204 4.8 0.6 1.0
CD1 B:ILE211 4.8 0.9 1.0
CD1 A:ILE211 4.8 1.0 1.0
CD A:GLU208 4.9 0.3 1.0
CD B:GLU208 4.9 1.0 1.0
CA B:GLU208 4.9 0.5 1.0
CA A:GLU208 4.9 0.7 1.0

Zinc binding site 2 out of 2 in 6iy6

Go back to Zinc Binding Sites List in 6iy6
Zinc binding site 2 out of 2 in the Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Cytosolic Aspartyl-Trna Synthetase (Drs) in Complex with Glutathion-S Transferase (Gst) Domains From Aminoacyl Trna Synthase Complex-Interacting Multifunctional Protein 2 (AIMP2) and Glutamyl-Prolyl-Trna Synthetase (Eprs) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn601

b:0.7
occ:1.00
 ND1 H:HIS204 3.5 0.3 1.0
OE1 G:GLU208 3.6 0.3 1.0
ND1 G:HIS204 3.7 0.8 1.0
OE1 H:GLU208 3.7 0.3 1.0
CE1 H:HIS204 3.8 0.9 1.0
CE1 G:HIS204 3.9 0.8 1.0
CB G:ARG207 4.0 0.7 1.0
CB H:ARG207 4.0 0.7 1.0
CD H:ARG207 4.2 0.6 1.0
CD G:ARG207 4.2 0.8 1.0
N H:GLU208 4.5 0.4 1.0
N G:GLU208 4.5 0.9 1.0
O H:HIS204 4.5 0.0 1.0
O G:HIS204 4.7 0.8 1.0
CD1 G:ILE211 4.7 0.0 1.0
CG H:HIS204 4.7 0.1 1.0
CG G:ARG207 4.7 0.4 1.0
CG H:ARG207 4.7 0.8 1.0
CD1 H:ILE211 4.9 0.3 1.0
CD G:GLU208 4.9 0.4 1.0
CD H:GLU208 4.9 0.7 1.0
CG G:HIS204 4.9 0.9 1.0
CA G:GLU208 4.9 0.9 1.0
CA H:GLU208 4.9 0.4 1.0
CA H:HIS204 5.0 0.7 1.0

Reference:

H.Hahn, S.H.Park, H.J.Kim, S.Kim, B.W.Han. The Drs-AIMP2-Eprs Subcomplex Acts As A Pivot in the Multi-Trna Synthetase Complex. Iucrj V. 6 958 2019.
ISSN: ESSN 2052-2525
PubMed: 31576228
DOI: 10.1107/S2052252519010790
Page generated: Tue Oct 29 00:37:11 2024

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