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Magnesium in PDB 1ide: Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination)

Enzymatic activity of Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination)

All present enzymatic activity of Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination):
1.1.1.42;

Protein crystallography data

The structure of Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination), PDB code: 1ide was solved by J.M.Bolduc, D.H.Dyer, W.G.Scott, P.Singer, R.M.Sweet, D.E.Koshland Junior, B.L.Stoddard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 105.100, 105.100, 150.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination) (pdb code 1ide). 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 Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination), PDB code: 1ide:

Magnesium binding site 1 out of 1 in 1ide

Go back to Magnesium Binding Sites List in 1ide
Magnesium binding site 1 out of 1 in the Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Isocitrate Dehydrogenase Y160F Mutant Steady-State Intermediate Complex (Laue Determination) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg417

b:1.0
occ:1.00
 OD1 A:ASP307 2.0 17.1 1.0
O A:HOH458 2.1 1.0 1.0
O2 A:ICT418 2.2 1.0 1.0
O A:HOH562 2.2 1.0 1.0
O7 A:ICT418 2.2 1.0 1.0
H2 A:HOH562 2.2 0.0 1.0
H1 A:HOH562 2.3 0.0 1.0
H1 A:HOH458 2.5 0.0 1.0
H2 A:HOH458 2.7 0.0 1.0
C1 A:ICT418 3.0 1.0 1.0
CG A:ASP307 3.2 15.6 1.0
C2 A:ICT418 3.2 1.0 1.0
HH12 A:ARG129 3.5 0.0 1.0
OD1 A:ASP311 3.7 24.5 1.0
OD2 A:ASP311 3.8 27.1 1.0
HH22 A:ARG129 3.8 0.0 1.0
CB A:ASP307 4.0 14.4 1.0
CG A:ASP311 4.0 23.1 1.0
OD2 A:ASP307 4.1 16.1 1.0
O6 A:ICT418 4.1 1.0 1.0
O1 A:ICT418 4.1 1.0 1.0
C3 A:ICT418 4.2 1.0 1.0
CA A:ASP307 4.3 15.1 1.0
O A:ASP307 4.3 12.3 1.0
C6 A:ICT418 4.4 1.0 1.0
HH12 A:ARG153 4.5 0.0 1.0
NH1 A:ARG129 4.5 17.7 1.0
C A:ASP307 4.5 12.0 1.0
NH2 A:ARG129 4.7 14.6 1.0
C4 A:ICT418 4.9 1.0 1.0

Reference:

J.M.Bolduc, D.H.Dyer, W.G.Scott, P.Singer, R.M.Sweet, D.E.Koshland Jr., B.L.Stoddard. Mutagenesis and Laue Structures of Enzyme Intermediates: Isocitrate Dehydrogenase. Science V. 268 1312 1995.
ISSN: ISSN 0036-8075
PubMed: 7761851
Page generated: Mon Dec 14 06:05:04 2020

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