Manganese in PDB 1xlj: 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: 1xlj 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 (°)	105.900, 105.900, 153.600, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

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

Manganese 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 Manganese with other atoms in the Mn 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:Mn399 b:22.1 occ:1.00 OE1 A:GLU216 1.9 17.8 1.0 OD2 A:ASP292 2.2 22.1 1.0 OD2 A:ASP244 2.2 19.9 1.0 O4 A:XYL400 2.4 24.0 1.0 OE2 A:GLU180 2.4 19.8 1.0 O2 A:XYL400 2.5 21.8 1.0 OE1 A:GLU180 3.0 22.3 1.0 CD A:GLU180 3.1 20.6 1.0 CD A:GLU216 3.2 16.3 1.0 CG A:ASP292 3.3 21.1 1.0 CG A:ASP244 3.3 19.5 1.0 C4 A:XYL400 3.4 22.4 1.0 C2 A:XYL400 3.5 21.4 1.0 C3 A:XYL400 3.7 21.8 1.0 O3 A:XYL400 3.8 19.9 1.0 CB A:ASP244 3.8 17.3 1.0 CB A:ASP292 3.9 19.7 1.0 O A:HOH502A 4.0 14.6 1.0 OE2 A:GLU216 4.0 13.9 1.0 O A:HOH500A 4.2 28.2 1.0 CG A:GLU216 4.2 14.0 1.0 CB A:GLU216 4.2 13.7 1.0 OD1 A:ASP292 4.3 20.2 1.0 CE1 A:HIS219 4.3 13.3 1.0 OD1 A:ASP244 4.4 20.4 1.0 CG A:GLU180 4.5 18.5 1.0 NE2 A:HIS219 4.5 14.8 1.0 ND2 A:ASN214 4.6 16.6 1.0 C5 A:XYL400 4.7 21.9 1.0 C1 A:XYL400 4.7 21.3 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn399 b:18.6 occ:1.00 OE1 B:GLU216 2.1 21.3 1.0 OE2 B:GLU180 2.1 17.1 1.0 OD2 B:ASP244 2.1 21.7 1.0 OD2 B:ASP292 2.2 20.2 1.0 O2 B:XYL400 2.3 17.6 1.0 O4 B:XYL400 2.3 19.4 1.0 CD B:GLU180 3.1 18.3 1.0 CD B:GLU216 3.2 18.2 1.0 CG B:ASP292 3.2 19.1 1.0 C2 B:XYL400 3.2 17.1 1.0 CG B:ASP244 3.3 20.4 1.0 OE1 B:GLU180 3.3 18.0 1.0 C4 B:XYL400 3.5 17.0 1.0 C3 B:XYL400 3.6 17.1 1.0 O3 B:XYL400 3.8 16.9 1.0 CB B:ASP292 3.8 18.4 1.0 O B:HOH528B 3.8 15.8 1.0 CB B:ASP244 3.8 18.1 1.0 OE2 B:GLU216 3.9 19.5 1.0 O B:HOH530B 3.9 21.9 1.0 OD1 B:ASP292 4.1 18.1 1.0 CG B:GLU216 4.2 14.1 1.0 CE1 B:HIS219 4.2 12.2 1.0 CB B:GLU216 4.2 13.2 1.0 OD1 B:ASP244 4.3 19.9 1.0 CG B:GLU180 4.4 18.4 1.0 NE2 B:HIS219 4.5 12.4 1.0 C1 B:XYL400 4.5 17.5 1.0 C5 B:XYL400 4.6 17.3 1.0 ND2 B:ASN214 4.7 17.6 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