Magnesium in PDB 7nu5: Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine

Enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine:
6.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine, PDB code: 7nu5 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) 56.79 / 2.58
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.469, 81.526, 227.154, 90, 90, 90
R / Rfree (%) 20.2 / 26.9

Other elements in 7nu5:

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine (pdb code 7nu5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine, PDB code: 7nu5:

Magnesium binding site 1 out of 1 in 7nu5

Go back to Magnesium Binding Sites List in 7nu5
Magnesium binding site 1 out of 1 in the Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with L- Leucine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:91.5
occ:1.00
O A:HOH1206 2.3 102.4 1.0
OE1 A:GLU210 3.8 71.8 1.0
CD A:GLU210 4.7 78.2 1.0
O A:LYS208 4.8 74.3 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: Thu Apr 6 17:46:54 2023

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