Magnesium in PDB 1cw7: Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate

All present enzymatic activity of Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate:
1.1.1.42;

The structure of Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate, PDB code: 1cw7 was solved by M.R.Stroud, J.Finer-Moore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	102.800, 102.800, 150.100, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 22.6

The binding sites of Magnesium atom in the Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate (pdb code 1cw7). 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 Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate, PDB code: 1cw7:

Magnesium binding site 1 out of 1 in the Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Low Temperature Structure of Wild-Type Idh Complexed with Mg- Isocitrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg418 b:17.5 occ:0.50 O2 A:ICT417 2.3 16.4 0.5 O A:HOH490 2.4 27.4 1.0 O7 A:ICT417 2.5 19.5 0.5 O A:HOH694 2.5 47.1 1.0 C1 A:ICT417 3.1 12.6 0.5 C2 A:ICT417 3.4 13.7 0.5 OD2 A:ASP307 3.7 11.4 1.0 O A:HOH506 3.8 27.9 1.0 O1 A:ICT417 4.0 18.9 0.5 OD2 A:ASP311 4.1 21.9 1.0 O6 A:ICT417 4.2 12.8 0.5 OD1 A:ASP311 4.3 20.7 1.0 C6 A:ICT417 4.4 14.4 0.5 C3 A:ICT417 4.5 13.9 0.5 CG A:ASP311 4.6 19.3 1.0 O A:THR338 4.7 24.3 1.0 CG A:ASP307 4.8 13.1 1.0

D.B.Cherbavaz, M.E.Lee, R.M.Stroud, D.E.Koshland Jr.. Active Site Water Molecules Revealed in the 2.1 A Resolution Structure of A Site-Directed Mutant of Isocitrate Dehydrogenase. J.Mol.Biol. V. 295 377 2000.
ISSN: ISSN 0022-2836
PubMed: 10623532
DOI: 10.1006/JMBI.1999.3195