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Magnesium in PDB 1zm7: Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp

Enzymatic activity of Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp

All present enzymatic activity of Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp:
2.7.1.145;

Protein crystallography data

The structure of Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp, PDB code: 1zm7 was solved by M.Welin, T.Skovgaard, W.Knecht, D.Berenstein, B.Munch-Petersen, J.Piskur, H.Eklund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.72 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.040, 119.270, 68.388, 90.00, 92.59, 90.00
R / Rfree (%) 21.2 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp (pdb code 1zm7). 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 D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp, PDB code: 1zm7:

Magnesium binding site 1 out of 1 in 1zm7

Go back to Magnesium Binding Sites List in 1zm7
Magnesium binding site 1 out of 1 in the Crystal Structure of D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp


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 D. Melanogaster Deoxyribonucleoside Kinase Mutant N64D in Complex with Dttp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg400

b:46.2
occ:1.00
 O1B D:TTP303 2.0 26.1 1.0
OG1 D:THR34 2.0 34.3 1.0
O D:HOH446 2.1 37.2 1.0
OE2 D:GLU52 2.2 43.2 1.0
O3G D:TTP303 2.4 25.8 1.0
OE2 D:GLU104 2.9 30.1 1.0
CB D:THR34 3.0 33.3 1.0
CD D:GLU52 3.1 42.1 1.0
PB D:TTP303 3.2 25.1 1.0
PG D:TTP303 3.3 27.9 1.0
OE1 D:GLU52 3.4 41.1 1.0
O3B D:TTP303 3.5 27.3 1.0
NH2 D:ARG169 3.7 28.4 1.0
CD D:GLU104 3.8 30.5 1.0
O1G D:TTP303 3.8 26.6 1.0
OE1 D:GLU104 3.9 30.2 1.0
CG2 D:THR34 3.9 33.5 1.0
O D:HOH453 4.0 31.0 1.0
N D:THR34 4.1 31.2 1.0
O D:HOH434 4.1 27.2 1.0
O3A D:TTP303 4.1 26.0 1.0
CA D:THR34 4.1 33.4 1.0
NH1 D:ARG167 4.3 29.1 1.0
O2B D:TTP303 4.3 25.9 1.0
CG D:GLU52 4.5 34.8 1.0
O2G D:TTP303 4.6 25.7 1.0
CA D:GLU52 4.8 31.4 1.0
CB D:GLU52 4.9 32.5 1.0
CZ D:ARG169 4.9 29.9 1.0
O D:HOH436 4.9 30.0 1.0

Reference:

M.Welin, T.Skovgaard, W.Knecht, C.Zhu, D.Berenstein, B.Munch-Petersen, J.Piskur, H.Eklund. Structural Basis For the Changed Substrate Specificity of Drosophila Melanogaster Deoxyribonucleoside Kinase Mutant N64D. Febs J. V. 272 3733 2005.
ISSN: ISSN 1742-464X
PubMed: 16008571
DOI: 10.1111/J.1742-4658.2005.04803.X
Page generated: Sun Aug 10 08:53:33 2025

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