Magnesium in PDB 1xlb: 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: 1xlb 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 (°)	105.300, 105.300, 153.500, 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 1xlb). 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: 1xlb:
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:22.2 occ:1.00 OE1 A:GLU216 2.0 24.7 1.0 OD2 A:ASP244 2.2 20.0 1.0 OE2 A:GLU180 2.3 21.3 1.0 OD2 A:ASP292 2.3 18.8 1.0 CD A:GLU180 3.0 19.7 1.0 CD A:GLU216 3.2 21.9 1.0 OE1 A:GLU180 3.2 20.3 1.0 O A:HOH612A 3.3 31.0 1.0 O A:HOH639A 3.3 31.2 1.0 CG A:ASP292 3.4 17.7 1.0 CG A:ASP244 3.4 19.2 1.0 O A:HOH514A 3.7 32.4 1.0 CB A:ASP244 3.9 17.4 1.0 CB A:ASP292 3.9 17.7 1.0 OE2 A:GLU216 4.1 22.8 1.0 CB A:GLU216 4.1 17.4 1.0 O A:HOH499A 4.1 34.5 1.0 CG A:GLU180 4.1 18.4 1.0 CG A:GLU216 4.2 18.8 1.0 O A:HOH620A 4.3 24.5 1.0 CE1 A:HIS219 4.3 17.4 1.0 OD1 A:ASP292 4.4 18.8 1.0 OD1 A:ASP244 4.4 20.8 1.0 ND2 A:ASN214 4.4 17.4 1.0 NE2 A:HIS219 4.5 17.4 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:21.8 occ:1.00 OE1 B:GLU216 2.2 22.9 1.0 OD2 B:ASP292 2.3 23.8 1.0 OD2 B:ASP244 2.3 24.4 1.0 OE2 B:GLU180 2.3 21.0 1.0 CD B:GLU180 3.1 19.1 1.0 O B:HOH634B 3.1 29.3 1.0 O B:HOH631B 3.2 34.9 1.0 OE1 B:GLU180 3.3 19.8 1.0 CG B:ASP292 3.3 22.6 1.0 CD B:GLU216 3.4 21.4 1.0 CG B:ASP244 3.5 21.8 1.0 O B:HOH511B 3.7 56.8 1.0 O B:HOH497B 3.9 37.5 1.0 CB B:ASP292 3.9 22.9 1.0 O B:HOH694B 4.0 54.5 1.0 CB B:ASP244 4.0 18.9 1.0 CG B:GLU216 4.3 19.2 1.0 CB B:GLU216 4.3 17.4 1.0 CG B:GLU180 4.3 17.9 1.0 CE1 B:HIS219 4.3 17.4 1.0 OD1 B:ASP292 4.3 21.2 1.0 OE2 B:GLU216 4.4 23.5 1.0 OD1 B:ASP244 4.4 22.0 1.0 NE2 B:HIS219 4.5 17.4 1.0 ND2 B:ASN214 4.6 17.9 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