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Magnesium in PDB 2hxd: Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium

Enzymatic activity of Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium

All present enzymatic activity of Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium:
3.5.4.30;

Protein crystallography data

The structure of Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium, PDB code: 2hxd was solved by J.H.Bynck, E.Johansson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.75 / 2.30
Space group I 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 171.513, 171.513, 171.513, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium (pdb code 2hxd). 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 Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium, PDB code: 2hxd:

Magnesium binding site 1 out of 1 in 2hxd

Go back to Magnesium Binding Sites List in 2hxd
Magnesium binding site 1 out of 1 in the Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bifunctional Dctp Deaminase-Dutpase Mutant Enzyme Variant E145A From Methanocaldococcus Jannaschii in Complex with Alpha,Beta-Imido Dutp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg205

b:39.5
occ:1.00
 O1A A:DUP206 2.2 31.2 1.0
O A:HOH306 2.2 31.4 1.0
O1G A:DUP206 2.2 35.1 1.0
O A:HOH260 2.3 32.3 1.0
O1B A:DUP206 2.4 27.3 1.0
O A:HOH218 3.4 27.6 1.0
PB A:DUP206 3.4 28.3 1.0
PA A:DUP206 3.5 31.1 1.0
PG A:DUP206 3.5 32.9 1.0
O A:HOH265 3.6 28.4 1.0
O3B A:DUP206 3.8 35.0 1.0
N3A A:DUP206 3.9 29.4 1.0
O3G A:DUP206 4.0 34.3 1.0
O2A A:DUP206 4.3 32.5 1.0
O A:HOH219 4.5 27.9 1.0
O5' A:DUP206 4.7 31.8 1.0
O2B A:DUP206 4.8 31.4 1.0
O2G A:DUP206 4.8 34.8 1.0
C5' A:DUP206 4.9 33.3 1.0
O A:HOH292 5.0 32.4 1.0

Reference:

J.H.Bynck, M.Willemoes, S.Larsen, E.Johansson. Structural Evidence For A Concerted Bifunctionality in Dctp Deaminase-Dutpase From Methanocaldococcus Jannaschii To Be Published.
Page generated: Mon Dec 14 07:26:37 2020

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