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Magnesium in PDB 2j4q: Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp

Enzymatic activity of Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp

All present enzymatic activity of Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp:
3.5.4.13;

Protein crystallography data

The structure of Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp, PDB code: 2j4q was solved by E.Johansson, M.Thymark, J.H.Bynck, M.Fanoe, S.Larsen, M.Willemoes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.60
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.594, 61.594, 344.766, 90.00, 90.00, 120.00
R / Rfree (%) 24.7 / 30.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp (pdb code 2j4q). 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 A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp, PDB code: 2j4q:

Magnesium binding site 1 out of 1 in 2j4q

Go back to Magnesium Binding Sites List in 2j4q
Magnesium binding site 1 out of 1 in the Crystal Structure of A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme 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 A E138A Escherichia Coli Dctp Deaminase Mutant Enzyme in Complex with Dttp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg195

b:50.8
occ:1.00
O1G B:TTP194 2.5 66.5 1.0
O2A B:TTP194 2.8 57.1 1.0
NH1 B:ARG126 3.0 30.0 1.0
NH2 B:ARG126 3.4 29.9 1.0
CZ B:ARG126 3.7 31.4 1.0
PG B:TTP194 3.8 67.0 1.0
PA B:TTP194 3.8 57.7 1.0
O1A B:TTP194 4.0 56.3 1.0
O3B B:TTP194 4.0 64.3 1.0
O3G B:TTP194 4.5 66.7 1.0
O3A B:TTP194 4.6 58.6 1.0
O2G B:TTP194 4.9 66.9 1.0

Reference:

E.Johansson, M.Thymark, J.H.Bynck, M.Fanoe, S.Larsen, M.Willemoes. Regulation of Dctp Deaminase From Escherichia Coli By Nonallosteric Dttp Binding to An Inactive Form of the Enzyme Febs J. V. 274 4188 2007.
ISSN: ISSN 1742-464X
PubMed: 17651436
DOI: 10.1111/J.1742-4658.2007.05945.X
Page generated: Wed Aug 14 00:24:47 2024

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