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

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

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

Protein crystallography data

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

Resolution Low / High (Å) 51.281 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.562, 102.562, 150.645, 90.00, 90.00, 90.00
R / Rfree (%) 16.31 / 19.15

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 4bnp

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


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 and Magnesium(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:27.3
occ:1.00
 OD1 A:ASP307 2.0 14.1 1.0
O A:HOH2439 2.1 19.3 1.0
O7 A:ICT502 2.1 22.5 1.0
O1 A:ICT502 2.2 25.9 1.0
O A:HOH2231 2.3 18.8 1.0
C1 A:ICT502 3.0 23.1 1.0
C2 A:ICT502 3.0 18.9 1.0
CG A:ASP307 3.2 14.7 1.0
OD2 A:ASP307 3.6 13.3 1.0
OD1 A:ASP311 3.9 20.5 1.0
O A:HOH2230 4.0 30.0 1.0
C6 A:ICT502 4.0 21.1 1.0
C3 A:ICT502 4.1 22.7 1.0
OD2 A:ASP311 4.1 21.3 1.0
O A:HOH2440 4.2 16.6 1.0
O2 A:ICT502 4.2 26.0 1.0
O A:HOH2526 4.2 31.8 1.0
CG A:ASP311 4.2 23.7 1.0
O6 A:ICT502 4.3 15.7 1.0
O A:ASP307 4.3 10.6 1.0
NH1 A:ARG129 4.3 22.7 1.0
O5 A:ICT502 4.4 16.0 1.0
CB A:ASP307 4.4 13.6 1.0
CA A:ASP307 4.6 12.7 1.0
NH1 A:ARG153 4.8 11.1 1.0
C A:ASP307 4.8 12.8 1.0
C4 A:ICT502 4.9 30.1 1.0

Reference:

S.P.Miller, S.Goncalves, P.M.Matias, A.M.Dean. Evolution of A Transition State: Role of LYS100 in the Active Site of Isocitrate Dehydrogenase. Chembiochem V. 15 1145 2014.
ISSN: ISSN 1439-4227
PubMed: 24797066
DOI: 10.1002/CBIC.201400040
Page generated: Thu Aug 15 16:30:08 2024

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