Magnesium in PDB 3h6d: Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant

All present enzymatic activity of Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant:
3.6.1.23;

The structure of Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant, PDB code: 3h6d was solved by I.Leveles, V.Harmat, G.Nagy, E.Takacs, A.Lopata, J.Toth, B.G.Vertessy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.16 / 1.80
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	55.228, 55.228, 83.650, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 20.7

The binding sites of Magnesium atom in the Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant (pdb code 3h6d). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant, PDB code: 3h6d:

Magnesium binding site 1 out of 1 in the Structure of the Mycobacterium Tuberculosis Dutpase D28N Mutant


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 Dutpase D28N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg200 b:35.8 occ:1.00 O1A A:DUP201 2.0 45.7 1.0 O2G A:DUP201 2.1 51.0 1.0 O1B A:DUP201 2.3 43.0 1.0 PB A:DUP201 3.3 45.6 1.0 PA A:DUP201 3.3 43.3 1.0 PG A:DUP201 3.4 53.5 1.0 O A:HOH245 3.5 33.3 1.0 N3A A:DUP201 3.6 43.9 1.0 O3B A:DUP201 3.7 49.6 1.0 O1G A:DUP201 4.0 50.6 1.0 O5' A:DUP201 4.3 38.1 1.0 C5' A:DUP201 4.4 29.6 1.0 O2A A:DUP201 4.5 41.8 1.0 O3G A:DUP201 4.6 49.2 1.0 O A:HOH197 4.7 16.5 1.0 O2B A:DUP201 4.7 38.5 1.0 OD2 A:ASP83 4.9 18.8 1.0

E.Takacs, G.Nagy, I.Leveles, V.Harmat, A.Lopata, J.Toth, B.G.Vertessy. Direct Contacts Between Conserved Motifs of Different Subunits Provide Major Contribution to Active Site Organization in Human and Mycobacterial Dutpases. Febs Lett. V. 584 3047 2010.
ISSN: ISSN 0014-5793
PubMed: 20493855
DOI: 10.1016/J.FEBSLET.2010.05.018