Magnesium in PDB 1r67: Y104A Mutant of E.Coli Ipp Isomerase

All present enzymatic activity of Y104A Mutant of E.Coli Ipp Isomerase:
5.3.3.2;

The structure of Y104A Mutant of E.Coli Ipp Isomerase, PDB code: 1r67 was solved by J.Wouters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.77
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.648, 71.648, 61.327, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 27.2

The binding sites of Magnesium atom in the Y104A Mutant of E.Coli Ipp Isomerase (pdb code 1r67). 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 Y104A Mutant of E.Coli Ipp Isomerase, PDB code: 1r67:

Magnesium binding site 1 out of 1 in the Y104A Mutant of E.Coli Ipp Isomerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Y104A Mutant of E.Coli Ipp Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:25.0 occ:1.00 O A:HOH307 2.2 22.2 1.0 OE1 A:GLU87 2.2 40.7 1.0 O A:CYS67 2.3 22.6 1.0 O A:HOH364 2.4 30.5 1.0 CD A:GLU87 3.1 30.5 1.0 O A:HOH355 3.3 39.1 0.5 OE2 A:GLU87 3.3 26.1 1.0 C A:CYS67 3.4 20.6 1.0 O A:HOH406 3.8 43.2 0.5 NH2 A:ARG83 3.8 52.5 1.0 N A:CYS67 3.9 22.9 1.0 NE A:ARG83 4.1 33.6 1.0 O A:HOH415 4.2 39.7 1.0 CA A:CYS67 4.3 22.4 1.0 OE1 A:GLU135 4.4 27.8 1.0 N A:GLY68 4.4 22.2 1.0 CA A:GLY68 4.4 29.9 1.0 O A:HOH308 4.4 20.4 1.0 CZ A:ARG83 4.4 44.4 1.0 SG A:CYS67 4.4 50.8 1.0 CG A:GLU87 4.5 23.2 1.0 NH1 A:ARG51 4.6 19.6 1.0 O A:HOH330 4.6 24.5 1.0 CG2 A:VAL66 4.7 33.9 1.0 CB A:CYS67 4.9 31.6 1.0

J.De Ruyck, V.Durisotti, Y.Oudjama, J.Wouters. Structural Role For Tyr-104 in Escherichia Coli Isopentenyl-Diphosphate Isomerase: Site-Directed Mutagenesis, Enzymology, and Protein Crystallography. J.Biol.Chem. V. 281 17864 2006.
ISSN: ISSN 0021-9258
PubMed: 16617181
DOI: 10.1074/JBC.M601851200