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Magnesium in PDB 4ajb: 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp

Enzymatic activity of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp

All present enzymatic activity of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp:
1.1.1.42;

Protein crystallography data

The structure of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp, PDB code: 4ajb was solved by S.Goncalves, S.P.Miller, M.A.Carrondo, A.M.Dean, P.M.Matias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.744 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 103.054, 103.054, 150.339, 90.00, 90.00, 90.00
R / Rfree (%) 16.63 / 18.05

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp (pdb code 4ajb). 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 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp, PDB code: 4ajb:

Magnesium binding site 1 out of 1 in 4ajb

Go back to Magnesium Binding Sites List in 4ajb
Magnesium binding site 1 out of 1 in the 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II) and Thionadp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:25.1
occ:1.00
 OD1 A:ASP307 2.1 19.3 1.0
O A:HOH2199 2.2 19.3 1.0
O A:HOH2393 2.2 22.6 1.0
O2 A:ICT502 2.3 22.1 1.0
O7 A:ICT502 2.3 22.1 1.0
C1 A:ICT502 3.0 24.0 1.0
CG A:ASP307 3.1 20.6 1.0
C2 A:ICT502 3.2 22.2 1.0
OD2 A:ASP307 3.6 19.8 1.0
OD1 A:ASP311 3.9 25.5 1.0
O A:HOH2395 4.1 28.9 1.0
C6 A:ICT502 4.1 21.8 1.0
O A:ASP307 4.1 18.1 1.0
NH1 A:ARG129 4.2 23.6 1.0
O1 A:ICT502 4.2 26.4 1.0
O6 A:ICT502 4.3 22.0 1.0
C3 A:ICT502 4.3 23.4 1.0
O A:HOH2484 4.3 25.1 1.0
CG A:ASP311 4.3 23.3 1.0
CB A:ASP307 4.4 16.7 1.0
OD2 A:ASP311 4.4 24.9 1.0
O5 A:ICT502 4.4 22.6 1.0
CA A:ASP307 4.5 17.5 1.0
C A:ASP307 4.6 19.4 1.0
NH1 A:ARG153 4.7 21.1 1.0

Reference:

S.Goncalves, S.P.Miller, M.A.Carrondo, A.M.Dean, P.M.Matias. Induced Fit and the Catalytic Mechanism of Isocitrate Dehydrogenase. Biochemistry V. 51 7098 2012.
ISSN: ISSN 0006-2960
PubMed: 22891681
DOI: 10.1021/BI300483W
Page generated: Thu Aug 15 14:33:43 2024

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