Magnesium in PDB 7nu9: Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp and L-Leucinol

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

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs in Complex with Atp and L-Leucinol, PDB code: 7nu9 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)	76.59 / 2.17
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.802, 81.894, 216.282, 90, 90, 90
R / Rfree (%)	19.4 / 24.9

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs 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 in Complex with Atp and L-Leucinol (pdb code 7nu9). 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 in Complex with Atp and L-Leucinol, PDB code: 7nu9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs 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 in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:22.9 occ:1.00 O A:HOH1254 2.0 22.6 1.0 O2A A:ATP1002 2.1 22.2 1.0 O A:HOH1202 2.1 20.2 1.0 O1G A:ATP1002 2.1 21.5 1.0 O A:HOH1195 2.2 21.2 1.0 O2B A:ATP1002 2.2 18.9 1.0 PB A:ATP1002 3.3 26.6 1.0 PG A:ATP1002 3.3 29.4 1.0 PA A:ATP1002 3.4 25.9 1.0 O3B A:ATP1002 3.4 29.1 1.0 O3A A:ATP1002 3.6 24.0 1.0 NZ A:LYS634 3.7 34.2 1.0 O A:HOH1168 3.9 35.6 1.0 OXT A:DCL1004 4.0 23.7 1.0 O5' A:ATP1002 4.0 25.0 1.0 O A:HOH1284 4.2 36.3 1.0 O2G A:ATP1002 4.2 27.0 1.0 NH1 A:ARG178 4.4 26.4 1.0 O3G A:ATP1002 4.4 29.4 1.0 O1A A:ATP1002 4.6 21.6 1.0 O1B A:ATP1002 4.6 26.5 1.0 OE2 A:GLU546 4.6 38.8 1.0 C A:DCL1004 4.7 20.1 1.0 CD2 A:TYR43 4.8 20.1 1.0 CE2 A:TYR43 4.9 19.9 1.0 CE A:LYS634 5.0 33.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Neisseria Gonorrhoeae Leurs 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 in Complex with Atp and L-Leucinol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1007 b:55.6 occ:1.00 O A:HOH1332 2.3 45.2 1.0 O A:HOH1243 2.5 53.6 1.0 O A:HOH1151 4.4 36.3 1.0 O A:HOH1191 4.5 38.6 1.0 OE1 A:GLU210 4.6 38.8 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