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Magnesium in PDB 1idc: Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography

Enzymatic activity of Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography

All present enzymatic activity of Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography:
1.1.1.42;

Protein crystallography data

The structure of Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography, PDB code: 1idc 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 (%) 16.9 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography (pdb code 1idc). 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 From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography, PDB code: 1idc:

Magnesium binding site 1 out of 1 in 1idc

Go back to Magnesium Binding Sites List in 1idc
Magnesium binding site 1 out of 1 in the Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Isocitrate Dehydrogenase From E.Coli (Mutant K230M), Steady-State Intermediate Complex Determined By Laue Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg417

b:30.7
occ:1.00
 OD1 A:ASP307 2.0 12.9 1.0
O5 A:OXS418 2.2 28.7 1.0
O7 A:OXS418 2.5 31.8 1.0
C5 A:OXS418 2.8 35.0 1.0
C6 A:OXS418 3.0 38.5 1.0
OD2 A:ASP311 3.1 27.3 1.0
CG A:ASP307 3.2 9.0 1.0
CG A:ASP311 3.7 22.4 1.0
OD1 A:ASP311 3.8 25.9 1.0
OD2 A:ASP307 3.8 18.4 1.0
O A:ASP307 4.1 13.7 1.0
C2 A:OXS418 4.1 31.5 1.0
O6 A:OXS418 4.2 37.6 1.0
CB A:ASP307 4.3 9.3 1.0
C1 A:OXS418 4.5 33.4 1.0
CA A:ASP307 4.5 7.5 1.0
C A:ASP307 4.5 12.0 1.0
C3 A:OXS418 4.7 29.7 1.0
NH1 A:ARG153 4.8 11.8 1.0
NH2 A:ARG129 4.8 22.9 1.0
O2 A:OXS418 4.8 31.0 1.0
O1 A:OXS418 4.9 36.2 1.0
CB A:ASP311 5.0 17.2 1.0
OH A:TYR160 5.0 18.4 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: Tue Aug 13 04:57:36 2024

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