Aluminium in PDB 1xlh: 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: 1xlh 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 (°)	105.800, 105.800, 153.500, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

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

Aluminium 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 Aluminium with other atoms in the Al 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:Al399 b:6.1 occ:1.00 O A:HOH691A 2.0 32.5 1.0 OD2 A:ASP244 2.0 23.7 1.0 OE1 A:GLU216 2.1 23.4 1.0 OD2 A:ASP292 2.1 18.1 1.0 OE2 A:GLU180 2.3 23.7 1.0 CG A:ASP244 3.2 23.5 1.0 CD A:GLU180 3.2 23.9 1.0 CG A:ASP292 3.3 18.0 1.0 CD A:GLU216 3.4 21.8 1.0 OE1 A:GLU180 3.4 24.8 1.0 O A:HOH681B 3.5 28.1 1.0 O A:HOH682B 3.8 28.4 1.0 CB A:ASP244 3.9 22.1 1.0 O A:HOH680B 3.9 37.8 1.0 CB A:ASP292 3.9 17.7 1.0 O A:HOH498A 4.0 33.6 1.0 OD1 A:ASP244 4.1 24.3 1.0 OD1 A:ASP292 4.3 19.0 1.0 CG A:GLU216 4.3 19.2 1.0 OE2 A:GLU216 4.3 19.9 1.0 CB A:GLU216 4.3 16.8 1.0 O A:HOH684B 4.3 30.5 1.0 CE1 A:HIS219 4.4 12.5 1.0 NE2 A:HIS219 4.5 12.3 1.0 CG A:GLU180 4.5 21.2 1.0 ND2 A:ASN214 4.6 17.9 1.0

Aluminium 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 Aluminium with other atoms in the Al 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:Al399 b:6.1 occ:1.00 OD2 B:ASP244 2.0 20.3 1.0 O B:HOH691B 2.0 32.9 1.0 OE1 B:GLU216 2.1 16.8 1.0 OD2 B:ASP292 2.1 22.5 1.0 OE2 B:GLU180 2.4 21.1 1.0 O B:HOH676B 3.1 29.0 1.0 CD B:GLU180 3.2 21.5 1.0 CG B:ASP244 3.2 19.2 1.0 CG B:ASP292 3.3 20.0 1.0 CD B:GLU216 3.3 16.2 1.0 OE1 B:GLU180 3.4 24.6 1.0 O B:HOH677B 3.7 29.9 1.0 CB B:ASP292 3.8 17.8 1.0 CB B:ASP244 3.9 19.9 1.0 O B:HOH673B 3.9 36.3 1.0 O B:HOH497B 4.1 30.5 1.0 OD1 B:ASP244 4.1 17.8 1.0 OD1 B:ASP292 4.2 19.8 1.0 CG B:GLU216 4.3 14.1 1.0 OE2 B:GLU216 4.3 14.6 1.0 CE1 B:HIS219 4.3 9.4 1.0 O B:HOH685B 4.4 34.8 1.0 CB B:GLU216 4.4 13.2 1.0 CG B:GLU180 4.4 20.2 1.0 NE2 B:HIS219 4.6 8.4 1.0 ND2 B:ASN214 4.6 14.3 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