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Magnesium in PDB 3hza: Crystal Structure of Dutpase H145W Mutant

Enzymatic activity of Crystal Structure of Dutpase H145W Mutant

All present enzymatic activity of Crystal Structure of Dutpase H145W Mutant:
3.6.1.23;

Protein crystallography data

The structure of Crystal Structure of Dutpase H145W Mutant, PDB code: 3hza was solved by I.Leveles, V.Harmat, I.Pecsi, J.Toth, B.G.Vertessy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.20
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 55.058, 55.058, 83.793, 90.00, 90.00, 120.00
R / Rfree (%) 11.7 / 15.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Dutpase H145W Mutant (pdb code 3hza). 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 Dutpase H145W Mutant, PDB code: 3hza:

Magnesium binding site 1 out of 1 in 3hza

Go back to Magnesium Binding Sites List in 3hza
Magnesium binding site 1 out of 1 in the Crystal Structure of Dutpase H145W 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 Dutpase H145W Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg200

b:10.5
occ:1.00
O2G A:DUP201 2.0 10.7 1.0
O1A A:DUP201 2.0 10.0 1.0
O1B A:DUP201 2.1 10.5 1.0
O A:HOH317 2.1 11.9 1.0
O A:HOH313 2.1 11.9 1.0
O A:HOH316 2.1 13.6 1.0
PB A:DUP201 3.1 12.2 1.0
PG A:DUP201 3.2 11.9 1.0
PA A:DUP201 3.3 10.8 1.0
O3B A:DUP201 3.4 13.3 1.0
N3A A:DUP201 3.6 13.9 1.0
O1G A:DUP201 3.8 13.8 1.0
O A:HOH324 4.2 18.4 1.0
C5' A:DUP201 4.3 10.4 1.0
O5' A:DUP201 4.3 10.2 1.0
O2A A:DUP201 4.4 13.3 1.0
O3G A:DUP201 4.4 12.3 1.0
O2B A:DUP201 4.5 12.2 1.0
OD2 A:ASP83 4.9 13.6 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: Mon Dec 14 08:15:15 2020

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