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

Enzymatic activity of 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;

Protein crystallography data

The structure of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift, PDB code: 1xlg 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, 153.200, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1xlg:

The structure of Mechanism For Aldose-Ketose Interconversion By D-Xylose Isomerase Involving Ring Opening Followed By A 1,2-Hydride Shift also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

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 1xlg). 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: 1xlg:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 1xlg

Go back to Aluminium Binding Sites List in 1xlg
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:17.4
occ:1.00
 OD2 A:ASP244 1.8 22.1 1.0
OE1 A:GLU216 1.8 22.2 1.0
O4 A:XYL400 1.8 33.6 1.0
OD2 A:ASP292 1.9 14.9 1.0
OE2 A:GLU180 2.0 20.1 1.0
O2 A:XYL400 2.2 30.9 1.0
CD A:GLU180 2.9 20.0 1.0
C4 A:XYL400 2.9 33.0 1.0
CD A:GLU216 3.0 21.7 1.0
CG A:ASP244 3.0 23.8 1.0
C2 A:XYL400 3.0 32.6 1.0
OE1 A:GLU180 3.1 20.7 1.0
CG A:ASP292 3.1 16.9 1.0
C3 A:XYL400 3.3 33.1 1.0
OE2 A:GLU216 3.7 22.6 1.0
CB A:ASP244 3.7 22.6 1.0
O3 A:XYL400 3.8 35.8 1.0
CB A:ASP292 3.8 18.1 1.0
OD1 A:ASP244 3.9 25.6 1.0
OD1 A:ASP292 4.1 17.0 1.0
CG A:GLU216 4.2 18.8 1.0
C5 A:XYL400 4.2 32.4 1.0
CG A:GLU180 4.2 17.0 1.0
O A:HOH498A 4.2 25.5 1.0
MG A:MG398 4.3 22.4 1.0
CE1 A:HIS219 4.3 11.0 1.0
C1 A:XYL400 4.4 32.9 1.0
CB A:GLU216 4.4 16.6 1.0
NE2 A:HIS219 4.5 11.3 1.0
ND2 A:ASN214 4.7 18.1 1.0
O1 A:XYL400 4.9 33.5 1.0

Aluminium binding site 2 out of 2 in 1xlg

Go back to Aluminium Binding Sites List in 1xlg
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:17.8
occ:1.00
 OD2 B:ASP244 1.8 20.8 1.0
OE1 B:GLU216 1.9 17.7 1.0
O2 B:XYL400 2.0 31.6 1.0
O4 B:XYL400 2.0 32.9 1.0
OD2 B:ASP292 2.0 18.1 1.0
OE2 B:GLU180 2.0 17.4 1.0
C2 B:XYL400 2.9 32.0 1.0
CD B:GLU180 2.9 16.9 1.0
C4 B:XYL400 3.0 31.9 1.0
CG B:ASP244 3.0 19.0 1.0
CD B:GLU216 3.0 16.6 1.0
CG B:ASP292 3.1 16.2 1.0
OE1 B:GLU180 3.2 19.2 1.0
C3 B:XYL400 3.2 32.3 1.0
CB B:ASP244 3.7 18.8 1.0
CB B:ASP292 3.7 15.2 1.0
O3 B:XYL400 3.7 34.7 1.0
OE2 B:GLU216 3.8 15.1 1.0
O B:HOH765B 3.9 28.0 1.0
OD1 B:ASP244 4.0 18.6 1.0
OD1 B:ASP292 4.1 14.8 1.0
CG B:GLU216 4.2 14.3 1.0
C1 B:XYL400 4.2 32.3 1.0
CG B:GLU180 4.3 14.6 1.0
C5 B:XYL400 4.3 30.8 1.0
CE1 B:HIS219 4.3 7.5 1.0
CB B:GLU216 4.4 14.0 1.0
MG B:MG398 4.5 24.5 1.0
NE2 B:HIS219 4.5 7.5 1.0
ND2 B:ASN214 4.7 15.4 1.0
O1 B:XYL400 4.9 31.5 1.0

Reference:

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
Page generated: Sun Jul 6 21:39:20 2025

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