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Magnesium in PDB 1dcm: Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A)

Protein crystallography data

The structure of Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A), PDB code: 1dcm was solved by P.Gouet, B.Fabry, V.Guillet, C.Birck, L.Mourey, D.Kahn, J.P.Samama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.92 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 115.600, 34.800, 66.900, 90.00, 119.40, 90.00
R / Rfree (%) 24.8 / 33.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A) (pdb code 1dcm). 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 Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A), PDB code: 1dcm:

Magnesium binding site 1 out of 1 in 1dcm

Go back to Magnesium Binding Sites List in 1dcm
Magnesium binding site 1 out of 1 in the Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Unphosphorylated Fixj-N with An Atypical Conformer (Monomer A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg127

b:35.7
occ:1.00
O B:ARG56 2.4 62.1 1.0
OD2 B:ASP54 2.5 53.1 1.0
OD1 B:ASP11 2.5 59.9 1.0
OD2 B:ASP11 2.7 60.2 1.0
CG B:ASP11 2.9 60.5 1.0
CG B:ASP54 3.5 51.2 1.0
C B:ARG56 3.6 62.9 1.0
OD1 B:ASP54 3.8 48.8 1.0
CB B:ASP11 4.4 56.7 1.0
CA B:MET57 4.5 65.8 1.0
N B:MET57 4.5 64.5 1.0
OD2 B:ASP10 4.5 59.7 1.0
CB B:ARG56 4.6 61.3 1.0
CA B:ARG56 4.6 61.7 1.0
CG B:MET57 4.6 58.3 1.0
CB B:ASP54 4.7 47.8 1.0
CG B:GLU12 4.8 59.5 1.0
N B:ARG56 5.0 60.5 1.0

Reference:

P.Gouet, B.Fabry, V.Guillet, C.Birck, L.Mourey, D.Kahn, J.P.Samama. Structural Transitions in the Fixj Receiver Domain. Structure Fold.Des. V. 7 1517 1999.
ISSN: ISSN 0969-2126
PubMed: 10647182
DOI: 10.1016/S0969-2126(00)88342-2
Page generated: Mon Dec 14 05:50:21 2020

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