Magnesium in PDB 1xlc: Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift

All present enzymatic activity of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift:
5.3.1.5;

The structure of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift, PDB code: 1xlc was solved by C.A.Collyer, K.Henrick, D.M.Blow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.50
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	105.600, 105.600, 152.700, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift (pdb code 1xlc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift, PDB code: 1xlc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg399 b:15.2 occ:1.00 OE1 A:GLU216 1.9 15.4 1.0 OD2 A:ASP244 1.9 18.3 1.0 OD2 A:ASP292 2.1 11.6 1.0 OE2 A:GLU180 2.1 15.8 1.0 O2 A:XYL400 2.3 20.5 1.0 O4 A:XYL400 2.3 21.9 1.0 CD A:GLU180 2.9 16.0 1.0 CG A:ASP244 3.1 17.2 1.0 CD A:GLU216 3.1 14.2 1.0 OE1 A:GLU180 3.1 15.4 1.0 CG A:ASP292 3.2 12.7 1.0 C2 A:XYL400 3.4 21.3 1.0 C4 A:XYL400 3.5 21.1 1.0 CB A:ASP244 3.6 16.2 1.0 C3 A:XYL400 3.8 21.8 1.0 CB A:ASP292 3.8 12.6 1.0 O A:HOH513 3.9 20.6 1.0 O3 A:XYL400 4.0 22.6 1.0 CB A:GLU216 4.0 11.3 1.0 CG A:GLU216 4.0 11.9 1.0 OE2 A:GLU216 4.0 13.5 1.0 OD1 A:ASP244 4.1 17.5 1.0 O A:HOH498 4.1 37.9 1.0 CE1 A:HIS219 4.2 10.6 1.0 OD1 A:ASP292 4.3 12.1 1.0 CG A:GLU180 4.3 14.3 1.0 NE2 A:HIS219 4.5 11.5 1.0 C1 A:XYL400 4.6 21.4 1.0 ND2 A:ASN214 4.6 16.0 1.0 C5 A:XYL400 4.7 20.4 1.0

Magnesium binding site 2 out of 2 in the Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg399 b:16.0 occ:1.00 OD2 B:ASP244 1.9 22.2 1.0 OD2 B:ASP292 2.1 15.8 1.0 OE1 B:GLU216 2.1 15.0 1.0 OE2 B:GLU180 2.1 14.2 1.0 O4 B:XYL400 2.2 21.1 1.0 O2 B:XYL400 2.2 22.1 1.0 CD B:GLU180 3.0 12.4 1.0 CG B:ASP244 3.1 20.4 1.0 OE1 B:GLU180 3.1 13.2 1.0 CG B:ASP292 3.2 14.8 1.0 C2 B:XYL400 3.3 21.9 1.0 C4 B:XYL400 3.3 20.4 1.0 CD B:GLU216 3.3 15.5 1.0 C3 B:XYL400 3.5 21.5 1.0 O3 B:XYL400 3.6 22.9 1.0 CB B:ASP244 3.7 18.9 1.0 CB B:ASP292 3.8 14.8 1.0 O B:HOH780 3.9 21.8 1.0 O B:HOH766 4.0 28.1 1.0 OD1 B:ASP244 4.0 21.0 1.0 OD1 B:ASP292 4.2 15.6 1.0 OE2 B:GLU216 4.2 15.4 1.0 CB B:GLU216 4.3 12.6 1.0 CG B:GLU216 4.3 13.9 1.0 CE1 B:HIS219 4.3 10.3 1.0 CG B:GLU180 4.3 11.9 1.0 C1 B:XYL400 4.5 22.6 1.0 C5 B:XYL400 4.6 20.2 1.0 ND2 B:ASN214 4.6 16.5 1.0 NE2 B:HIS219 4.6 9.6 1.0

C.A.Collyer, K.Henrick, D.M.Blow. Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift. J.Mol.Biol. V. 212 211 1990.
ISSN: ISSN 0022-2836
PubMed: 2319597
DOI: 10.1016/0022-2836(90)90316-E