Magnesium in PDB 7nu0: Crystal Structure of Neisseria Gonorrhoeae Leurs L550A Mutant in Complex with Atp and L-Leucinol

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs L550A Mutant in Complex with Atp and L-Leucinol:
6.1.1.4;

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs L550A Mutant in Complex with Atp and L-Leucinol, PDB code: 7nu0 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)	53.93 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.511, 81.441, 215.713, 90, 90, 90
R / Rfree (%)	17.9 / 21.4

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs L550A 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 L550A Mutant in Complex with Atp and L-Leucinol (pdb code 7nu0). 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 L550A Mutant in Complex with Atp and L-Leucinol, PDB code: 7nu0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550A 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 L550A Mutant in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:23.8 occ:1.00 O2G A:ATP1002 2.1 25.0 1.0 O A:HOH1381 2.1 26.8 1.0 O2A A:ATP1002 2.1 25.9 1.0 O A:HOH1396 2.1 22.9 1.0 O A:HOH1309 2.2 24.0 1.0 O2B A:ATP1002 2.2 22.1 1.0 PB A:ATP1002 3.2 24.6 1.0 PG A:ATP1002 3.2 27.3 1.0 O3B A:ATP1002 3.3 25.1 1.0 PA A:ATP1002 3.4 23.4 1.0 O3A A:ATP1002 3.6 23.7 1.0 O A:HOH1233 3.8 34.7 1.0 OXT A:DCL1004 3.9 24.0 1.0 O3G A:ATP1002 4.0 25.4 1.0 O5' A:ATP1002 4.0 24.3 1.0 O A:HOH1520 4.2 44.7 1.0 O A:HOH1284 4.3 38.4 1.0 O1G A:ATP1002 4.4 27.7 1.0 NH2 A:ARG178 4.4 25.3 1.0 NZ A:LYS634 4.5 25.8 1.0 O1B A:ATP1002 4.6 24.6 1.0 O1A A:ATP1002 4.6 23.8 1.0 C A:DCL1004 4.6 21.1 1.0 CD2 A:TYR43 4.7 21.4 1.0 OE2 A:GLU546 4.8 47.7 1.0 CE2 A:TYR43 4.8 23.3 1.0 CE A:LYS634 4.9 32.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs L550A 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 L550A Mutant in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1007 b:48.7 occ:1.00 O A:HOH1131 2.1 46.3 1.0 O A:HOH1250 2.1 40.2 1.0 OE1 A:GLU210 4.1 30.2 1.0 O A:LYS208 4.2 28.6 1.0 O A:HOH1207 4.6 34.8 1.0 CD A:GLU210 4.6 37.0 1.0 O A:HOH1501 4.7 45.4 1.0 CG A:GLU210 4.9 31.1 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