Magnesium in PDB 8qzh: Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis

The structure of Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis, PDB code: 8qzh was solved by S.Gavalda, C.Carivenc, L.Mourey, J.D.Pedelacq, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.99 / 1.70
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	46.169, 46.169, 181.66, 90, 90, 120
R / Rfree (%)	20.6 / 23.4

The binding sites of Magnesium atom in the Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis (pdb code 8qzh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis, PDB code: 8qzh:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis


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 Apo-Pptt From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:22.4 occ:1.00 OXT A:ACT301 2.1 27.9 1.0 O A:HOH421 2.2 27.2 1.0 OD1 A:ASP114 2.2 31.9 1.0 O A:HOH425 2.2 22.4 1.0 O A:HOH424 2.2 22.4 1.0 O A:HOH520 2.2 25.8 1.0 HZ3 A:LYS161 3.0 32.2 1.0 C A:ACT301 3.0 27.6 1.0 CG A:ASP114 3.1 27.8 1.0 HG1 A:THR92 3.1 24.4 1.0 OD2 A:ASP114 3.3 26.0 1.0 H2 A:ACT301 3.5 32.7 1.0 CH3 A:ACT301 3.7 27.2 1.0 O A:ACT301 3.8 29.8 1.0 NZ A:LYS161 3.8 26.8 1.0 OG1 A:THR92 3.8 20.4 1.0 H1 A:ACT301 3.9 32.7 1.0 HG3 A:GLU157 3.9 28.2 1.0 HZ1 A:LYS161 4.0 32.2 1.0 H A:ALA115 4.1 25.8 1.0 OE2 A:GLU116 4.1 31.2 1.0 HB3 A:GLU157 4.1 23.4 1.0 OE1 A:GLU157 4.3 26.6 1.0 HE3 A:LYS161 4.3 31.6 1.0 HZ2 A:LYS161 4.3 32.2 1.0 HA A:ASP114 4.4 27.3 1.0 O A:ALA115 4.4 23.3 1.0 O A:HOH462 4.4 35.2 1.0 CB A:ASP114 4.5 25.6 1.0 H A:HIS93 4.5 28.6 1.0 O A:HIS93 4.5 27.1 1.0 CE A:LYS161 4.5 26.3 1.0 HG2 A:GLU116 4.6 31.0 1.0 CG A:GLU157 4.6 23.5 1.0 HE2 A:LYS161 4.6 31.6 1.0 H3 A:ACT301 4.7 32.7 1.0 HB2 A:ASP114 4.7 30.8 1.0 CB A:GLU157 4.7 19.5 1.0 HB2 A:GLU157 4.8 23.4 1.0 N A:ALA115 4.8 21.5 1.0 HA A:THR92 4.8 27.8 1.0 CA A:ASP114 4.9 22.7 1.0 CD A:GLU157 4.9 26.4 1.0 CB A:THR92 5.0 23.0 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis


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 Apo-Pptt From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg305 b:28.6 occ:1.00 O A:HOH487 2.0 28.9 1.0 O A:VAL226 2.0 29.5 1.0 O A:HOH437 2.1 30.5 1.0 O A:HOH473 2.2 27.6 1.0 O A:HOH418 2.3 36.0 1.0 O A:ACT302 2.3 35.8 1.0 C A:VAL226 3.2 23.4 1.0 C A:ACT302 3.2 36.2 1.0 H A:VAL226 3.2 23.0 1.0 HB A:VAL226 3.5 25.1 1.0 OXT A:ACT302 3.5 36.8 1.0 HA A:LEU227 3.8 34.8 1.0 HH21 A:ARG211 3.9 90.9 1.0 N A:VAL226 3.9 19.2 1.0 HD23 A:LEU227 3.9 38.0 1.0 CA A:VAL226 3.9 21.4 1.0 CB A:VAL226 4.1 20.9 1.0 O A:ARG211 4.2 23.3 1.0 NH2 A:ARG211 4.2 75.8 1.0 N A:LEU227 4.2 29.1 1.0 HH22 A:ARG211 4.3 90.9 1.0 HB2 A:ARG211 4.3 50.0 1.0 O A:HOH511 4.4 23.0 1.0 HG12 A:VAL226 4.4 25.7 1.0 CA A:LEU227 4.5 29.0 1.0 CH3 A:ACT302 4.5 35.2 1.0 H2 A:ACT302 4.6 42.2 1.0 HG23 A:ILE225 4.7 30.3 1.0 HG2 A:PRO12 4.7 34.1 1.0 H1 A:ACT302 4.8 42.2 1.0 HA A:VAL226 4.9 25.7 1.0 CD2 A:LEU227 4.9 31.7 1.0 CG1 A:VAL226 4.9 21.4 1.0 HG11 A:VAL15 4.9 39.2 1.0 CZ A:ARG211 4.9 73.3 1.0 HA A:ILE225 5.0 28.0 1.0 HE A:ARG211 5.0 80.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Apo-Pptt From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg306 b:35.6 occ:1.00 O A:PRO139 2.2 49.4 1.0 O A:HOH481 2.2 33.6 1.0 O A:HOH452 2.3 42.9 1.0 O A:HOH497 2.3 38.4 1.0 O A:HOH515 2.3 53.0 1.0 C A:PRO139 3.3 39.0 1.0 HB2 A:ALA144 3.8 40.0 1.0 HA A:PRO139 3.8 41.6 1.0 O A:MET142 3.9 26.8 1.0 HA A:ARG140 4.0 39.3 1.0 CA A:PRO139 4.0 34.7 1.0 HB3 A:PRO139 4.2 40.5 1.0 N A:ARG140 4.4 36.1 1.0 H A:ALA144 4.4 36.2 1.0 HB2 A:PRO139 4.4 40.5 1.0 CB A:PRO139 4.5 33.8 1.0 CA A:ARG140 4.6 32.8 1.0 O A:HOH523 4.6 34.6 1.0 CB A:ALA144 4.7 33.4 1.0 N A:ALA144 4.8 30.2 1.0 C A:ARG140 4.9 29.0 1.0 H A:MET142 4.9 32.4 1.0 HA A:ALA144 5.0 36.9 1.0

S.Gavalda, A.Faille, S.Fioccola, M.C.Nguyen, C.Carivenc, K.Rottier, Y.Rufin, S.Saitta, G.Czaplicki, C.Guilhot, C.Chalut, M.Brut, L.Mourey, J.D.Pedelacq. Catalytic Cycle of Type II 4'-Phosphopantetheinyl Transferases Acs Catalysis V. 14 8561 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.3C06249