Magnesium in PDB 4bzx: Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps

All present enzymatic activity of Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps:
2.7.1.25;

The structure of Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps, PDB code: 4bzx was solved by O.Poyraz, B.Lohkamp, R.Schnell, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.26 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.820, 69.430, 79.370, 90.00, 90.00, 90.00
R / Rfree (%)	17.415 / 21.599

The binding sites of Magnesium atom in the Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps (pdb code 4bzx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps, PDB code: 4bzx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1624 b:32.0 occ:1.00 O A:HOH2014 2.0 30.0 1.0 O2B A:ANP1614 2.1 21.5 1.0 O2G A:ANP1614 2.1 22.4 0.5 O A:HOH2013 2.1 37.5 1.0 OG A:SER457 2.1 26.6 1.0 O A:HOH2015 2.1 35.5 1.0 CB A:SER457 3.1 22.9 1.0 PG A:ANP1614 3.2 23.2 0.5 PB A:ANP1614 3.2 22.6 1.0 N3B A:ANP1614 3.4 21.8 1.0 O3G A:ANP1614 3.8 16.0 0.5 O A:HOH2048 4.0 18.6 0.5 N A:SER457 4.1 18.2 1.0 O1A A:ANP1614 4.1 26.7 1.0 OD2 A:ASP478 4.1 28.9 1.0 NZ A:LYS562 4.1 56.9 1.0 O A:HOH2025 4.1 28.2 0.5 CA A:SER457 4.1 19.0 1.0 O3' A:ADX1613 4.3 33.3 1.0 O3A A:ANP1614 4.3 24.2 1.0 O1B A:ANP1614 4.4 21.4 1.0 OD1 A:ASP478 4.4 32.9 1.0 O1G A:ANP1614 4.4 23.1 0.5 O A:HOH2027 4.5 50.4 1.0 PA A:ANP1614 4.5 26.4 1.0 CG A:ASP478 4.7 30.4 1.0 O2A A:ANP1614 4.7 27.2 1.0 O A:HOH2060 4.8 40.4 1.0

Magnesium binding site 2 out of 2 in the Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Mycobacterium Tuberculosis Aps Kinase Cysc in Complex with Amppnp and Aps within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1622 b:51.4 occ:1.00 O B:HOH2008 1.8 41.3 1.0 O3G B:ANP1614 1.9 34.0 0.5 O B:HOH2010 2.2 28.2 0.5 O B:HOH2009 2.4 45.6 1.0 OG B:SER457 2.4 23.7 0.5 O2B B:ANP1614 2.4 30.1 1.0 PG B:ANP1614 3.0 37.5 0.5 N3B B:ANP1614 3.3 26.3 1.0 OG B:SER457 3.4 29.8 0.5 PB B:ANP1614 3.4 28.9 1.0 CB B:SER457 3.5 29.8 0.5 CB B:SER457 3.5 27.8 0.5 O B:HOH2022 3.5 36.5 0.5 O1G B:ANP1614 3.5 22.0 0.5 O B:HOH2021 3.6 27.3 0.5 NZ B:LYS562 4.1 65.6 1.0 OD2 B:ASP478 4.2 42.3 1.0 O3' B:ADX1613 4.2 48.7 1.0 O2G B:ANP1614 4.3 32.5 0.5 N B:SER457 4.3 27.0 1.0 O1A B:ANP1614 4.4 32.0 1.0 CA B:SER457 4.5 27.1 0.5 CA B:SER457 4.5 28.0 0.5 O1B B:ANP1614 4.5 27.0 1.0 OD1 B:ASP478 4.6 45.8 1.0 O3A B:ANP1614 4.6 32.0 1.0 CG B:ASP478 4.8 42.4 1.0 CE B:LYS456 4.9 24.1 1.0 NZ B:LYS456 4.9 24.8 1.0 PA B:ANP1614 5.0 32.4 1.0

O.Poyraz, B.Lohkamp, R.Schnell, G.Schneider. Structure and Function of the Aps Kinase Cysc of Mycobacterium Tuberculosis To Be Published.