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Magnesium in PDB 3i93: Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant:
3.6.1.23;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant, PDB code: 3i93 was solved by I.Leveles, V.Harmat, 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) 19.44 / 1.80
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 54.591, 54.591, 83.051, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 20.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant (pdb code 3i93). 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 Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant, PDB code: 3i93:

Magnesium binding site 1 out of 1 in 3i93

Go back to Magnesium Binding Sites List in 3i93
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Dutpase STOP138T Mutant


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 Mycobacterium Tuberculosis Dutpase STOP138T Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg200

b:16.8
occ:1.00
NE A:ARG64 4.2 20.4 1.0
OD1 A:ASP28 4.2 22.9 1.0
OE1 A:GLN113 4.3 21.9 1.0
NH2 A:ARG64 4.4 27.2 1.0
OD2 A:ASP28 4.6 25.9 1.0
O A:HOH337 4.6 21.3 1.0
NE2 A:GLN113 4.7 19.2 1.0
CD A:GLN113 4.8 21.7 1.0
CZ A:ARG64 4.8 25.4 1.0
CG A:ASP28 4.8 18.6 1.0

Reference:

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
Page generated: Mon Dec 14 08:16:24 2020

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