Zinc in PDB 7nu7: Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2

Enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2:
6.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2, PDB code: 7nu7 was solved by L.Pang, S.V.Strelkov, S.D.Weeks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.04 / 2.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.141, 82.728, 228.468, 90, 90, 90
R / Rfree (%) 20.6 / 26.4

Other elements in 7nu7:

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2 (pdb code 7nu7). 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 Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2, PDB code: 7nu7:

Zinc binding site 1 out of 1 in 7nu7

Go back to Zinc Binding Sites List in 7nu7
Zinc binding site 1 out of 1 in the Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2


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 Neisseria Gonorrhoeae Leurs in Complex with Atp in Conformation 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1004

b:49.6
occ:1.00
 SG A:CYS452 2.3 48.1 1.0
SG A:CYS449 2.3 42.7 1.0
SG A:CYS490 2.4 54.9 1.0
SG A:CYS493 2.4 52.6 1.0
CB A:CYS490 3.0 49.2 1.0
CB A:CYS493 3.1 45.7 1.0
CB A:CYS452 3.2 43.8 1.0
CB A:CYS449 3.3 40.9 1.0
N A:CYS493 3.6 48.5 1.0
N A:CYS452 3.9 45.8 1.0
CA A:CYS493 4.0 55.2 1.0
CA A:CYS452 4.2 40.9 1.0
CA A:CYS490 4.5 43.1 1.0
O A:HOH1134 4.5 55.8 1.0
CB A:LYS451 4.6 58.4 1.0
C A:CYS492 4.7 51.4 1.0
CB A:CYS492 4.7 60.4 1.0
CA A:CYS449 4.7 49.1 1.0
N A:GLY494 4.7 54.0 1.0
C A:CYS493 4.7 59.0 1.0
C A:LYS451 4.8 60.4 1.0

Reference:

L.Pang, V.Zanki, S.V.Strelkov, A.Van Aerschot, I.Gruic-Sovulj, S.D.Weeks. Partitioning of the Initial Catalytic Steps of Leucyl-Trna Synthetase Is Driven By An Active Site Peptide-Plane Flip. Commun Biol V. 5 883 2022.
ISSN: ESSN 2399-3642
PubMed: 36038645
DOI: 10.1038/S42003-022-03825-8
Page generated: Wed Oct 30 07:55:51 2024

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