Magnesium in PDB 2icj: The Crystal Structure of Human Isopentenyl Diphophate Isomerase

All present enzymatic activity of The Crystal Structure of Human Isopentenyl Diphophate Isomerase:
5.3.3.2;

The structure of The Crystal Structure of Human Isopentenyl Diphophate Isomerase, PDB code: 2icj was solved by W.Zheng, M.Bartlam, Z.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.831, 47.391, 116.619, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.9

The binding sites of Magnesium atom in the The Crystal Structure of Human Isopentenyl Diphophate Isomerase (pdb code 2icj). 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 The Crystal Structure of Human Isopentenyl Diphophate Isomerase, PDB code: 2icj:

Magnesium binding site 1 out of 1 in the The Crystal Structure of Human Isopentenyl Diphophate Isomerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Human Isopentenyl Diphophate Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:12.9 occ:1.00 OE2 A:GLU149 2.2 26.8 1.0 OE1 A:GLU147 2.2 21.2 1.0 NE2 A:HIS52 2.3 17.2 1.0 NE2 A:HIS41 2.3 18.2 1.0 O A:HOH589 2.3 36.8 1.0 OE2 A:GLU147 2.3 22.7 1.0 CD A:GLU147 2.6 22.0 1.0 CE1 A:HIS52 2.9 17.9 1.0 CE1 A:HIS41 3.1 18.6 1.0 CD A:GLU149 3.2 21.7 1.0 CD2 A:HIS41 3.4 22.2 1.0 CD2 A:HIS52 3.5 15.2 1.0 CG A:GLU149 3.7 24.1 1.0 CG A:GLU147 4.1 20.3 1.0 ND1 A:HIS52 4.2 15.1 1.0 ND1 A:HIS41 4.2 15.8 1.0 OE1 A:GLU149 4.3 19.6 1.0 CG A:HIS41 4.4 15.1 1.0 CG A:HIS52 4.5 13.6 1.0 ND1 A:HIS89 4.6 25.5 1.0 CB A:GLU149 4.8 20.2 1.0 CB A:ALA54 4.8 13.0 1.0 O A:HOH582 4.8 61.3 1.0 CB A:GLU147 4.9 17.4 1.0

W.Zheng, F.Sun, M.Bartlam, X.Li, R.Li, Z.Rao. The Crystal Structure of Human Isopentenyl Diphosphate Isomerase at 1.7 A Resolution Reveals Its Catalytic Mechanism in Isoprenoid Biosynthesis J.Mol.Biol. V. 366 1447 2007.
ISSN: ISSN 0022-2836
PubMed: 17250851
DOI: 10.1016/J.JMB.2006.12.055