Zinc in PDB 7nu3: Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol

Enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol:
6.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol, PDB code: 7nu3 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) 66.60 / 2.27
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.878, 82.214, 227.207, 90, 90, 90
R / Rfree (%) 20 / 24.9

Other elements in 7nu3:

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol 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 E169G Mutant in Complex with Atp and L-Leucinol (pdb code 7nu3). 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 E169G Mutant in Complex with Atp and L-Leucinol, PDB code: 7nu3:

Zinc binding site 1 out of 1 in 7nu3

Go back to Zinc Binding Sites List in 7nu3
Zinc binding site 1 out of 1 in the Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant in Complex with Atp and L-Leucinol


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 E169G Mutant in Complex with Atp and L-Leucinol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1004

b:46.1
occ:1.00
 SG A:CYS452 2.2 49.4 1.0
SG A:CYS449 2.2 40.8 1.0
SG A:CYS493 2.3 46.3 1.0
SG A:CYS490 2.3 46.6 1.0
CB A:CYS490 3.1 46.5 1.0
CB A:CYS452 3.2 52.9 1.0
CB A:CYS449 3.2 38.0 1.0
CB A:CYS493 3.3 40.5 1.0
N A:CYS493 3.8 44.2 1.0
N A:CYS452 3.9 43.5 1.0
CA A:CYS493 4.1 45.0 1.0
CA A:CYS452 4.2 35.6 1.0
CA A:CYS490 4.5 37.4 1.0
CB A:CYS492 4.5 59.2 1.0
CB A:LYS451 4.6 49.4 1.0
O A:HOH1138 4.6 48.2 1.0
CA A:CYS449 4.7 45.6 1.0
C A:CYS492 4.7 45.4 1.0
C A:LYS451 4.8 52.5 1.0
C A:CYS493 4.8 46.8 1.0
N A:GLY494 4.9 47.4 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 07:54:55 2024

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