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Manganese in PDB 3loj: Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant

Enzymatic activity of Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant:
3.6.1.23;

Protein crystallography data

The structure of Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant, PDB code: 3loj was solved by I.Leveles, V.Harmat, I.Pecsi, A.Lopata, B.G.Vertessy, J.Toth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.25
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 (%) 12.8 / 17.7

Other elements in 3loj:

The structure of Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant (pdb code 3loj). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant, PDB code: 3loj:

Manganese binding site 1 out of 1 in 3loj

Go back to Manganese Binding Sites List in 3loj
Manganese binding site 1 out of 1 in the Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Mycobacterium Tuberculosis Dutpase H145A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn156

b:13.8
occ:0.50
MG A:MG155 0.1 7.5 0.5
O2G A:DUP201 2.1 12.3 1.0
O1B A:DUP201 2.1 11.8 1.0
O1A A:DUP201 2.1 11.8 1.0
O A:HOH245 2.1 14.4 1.0
O A:HOH239 2.2 13.6 1.0
O A:HOH212 2.2 15.3 1.0
PB A:DUP201 3.2 15.0 1.0
PG A:DUP201 3.2 14.2 1.0
PA A:DUP201 3.4 13.3 1.0
O3B A:DUP201 3.5 17.8 1.0
N3A A:DUP201 3.6 16.2 1.0
O1G A:DUP201 3.8 18.9 1.0
C5' A:DUP201 4.3 12.0 1.0
O A:HOH227 4.4 19.1 1.0
O5' A:DUP201 4.4 11.3 1.0
O2A A:DUP201 4.4 17.8 1.0
O3G A:DUP201 4.5 14.5 1.0
O2B A:DUP201 4.5 14.8 1.0

Reference:

I.Pecsi, I.Leveles, V.Harmat, B.G.Vertessy, J.Toth. Aromatic Stacking Between Nucleobase and Enzyme Promotes Phosphate Ester Hydrolysis in Dutpase Nucleic Acids Res. V. 38 7179 2010.
ISSN: ISSN 0305-1048
PubMed: 20601405
DOI: 10.1093/NAR/GKQ584
Page generated: Sat Oct 5 16:50:25 2024

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