Magnesium in PDB 7nuc: Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol:
6.1.1.4;

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol, PDB code: 7nuc 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)	76.37 / 2.77
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.912, 81.588, 216.971, 90, 90, 90
R / Rfree (%)	18.5 / 26.4

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol (pdb code 7nuc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol, PDB code: 7nuc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol


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 L550G Mutant in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:12.2 occ:1.00 O2A A:ATP1002 2.1 17.8 1.0 O A:HOH1121 2.1 19.4 1.0 O A:HOH1126 2.2 18.3 1.0 O2G A:ATP1002 2.2 28.0 1.0 O2B A:ATP1002 2.6 20.3 1.0 O A:HOH1219 2.8 32.1 1.0 PA A:ATP1002 3.5 20.2 1.0 PG A:ATP1002 3.5 35.5 1.0 OXT A:DCL1004 3.6 22.1 1.0 PB A:ATP1002 3.7 28.7 1.0 O3B A:ATP1002 3.8 34.5 1.0 O3A A:ATP1002 3.9 29.5 1.0 O5' A:ATP1002 4.1 32.3 1.0 NH2 A:ARG178 4.1 22.0 1.0 O3G A:ATP1002 4.2 33.9 1.0 C A:DCL1004 4.3 24.4 1.0 OE2 A:GLU546 4.3 57.4 1.0 CD2 A:TYR43 4.3 19.4 1.0 CE2 A:TYR43 4.4 22.9 1.0 O1A A:ATP1002 4.6 23.2 1.0 O1G A:ATP1002 4.7 39.2 1.0 NZ A:LYS634 4.7 20.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Neisseria Gonorrhoeae Leurs L550G Mutant in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1007 b:64.9 occ:1.00 O A:HOH1210 2.2 51.8 1.0 O A:HOH1228 3.3 43.3 1.0 O A:LYS208 3.8 32.7 1.0 O A:HOH1155 4.4 29.8 1.0 OE1 A:GLU210 4.4 38.3 1.0 CG A:GLU210 4.8 29.6 1.0 CD A:GLU210 4.8 33.7 1.0 C A:LYS208 4.9 33.4 1.0

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