Manganese in PDB 1xic: Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase

All present enzymatic activity of Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase:
5.3.1.5;

The structure of Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase, PDB code: 1xic was solved by H.L.Carrell, J.P.Glusker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.00 / 1.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.900, 99.700, 102.900, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase (pdb code 1xic). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase, PDB code: 1xic:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn390 b:28.8 occ:1.00 OE2 A:GLU217 2.2 14.0 1.0 O A:HOH409 2.4 14.8 1.0 OD2 A:ASP255 2.4 21.5 1.0 OD1 A:ASP255 2.4 19.2 1.0 OD1 A:ASP257 2.5 11.2 1.0 NE2 A:HIS220 2.6 11.5 1.0 CG A:ASP255 2.8 18.9 1.0 CD A:GLU217 3.1 6.9 1.0 CD2 A:HIS220 3.1 5.6 1.0 CG A:ASP257 3.4 9.4 1.0 O A:HOH565 3.4 8.8 1.0 OE1 A:GLU217 3.5 9.9 1.0 OD2 A:ASP257 3.5 16.8 1.0 CE1 A:HIS220 3.7 7.5 1.0 O5 A:XLS389 4.0 26.3 1.0 ND2 A:ASN247 4.0 5.0 1.0 CB A:ASP255 4.2 7.4 1.0 O A:HOH412 4.3 10.6 1.0 CG A:HIS220 4.4 5.0 1.0 CG A:GLU217 4.5 5.0 1.0 ND1 A:HIS220 4.6 7.8 1.0 NZ A:LYS183 4.7 8.5 1.0 CE A:LYS183 4.7 5.0 1.0 C5 A:XLS389 4.7 29.4 1.0 O A:HOH615 4.8 23.0 1.0 OD2 A:ASP287 4.8 12.9 1.0 CB A:ASP257 4.8 5.0 1.0 MN A:MN391 4.9 18.0 1.0

Manganese binding site 2 out of 2 in the Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn391 b:18.0 occ:1.00 OD2 A:ASP287 2.2 12.9 1.0 OE1 A:GLU217 2.2 9.9 1.0 O3 A:XLS389 2.3 26.8 1.0 OE2 A:GLU181 2.3 24.0 1.0 O5 A:XLS389 2.3 26.3 1.0 OD2 A:ASP245 2.4 11.1 1.0 CD A:GLU181 3.1 16.4 1.0 C5 A:XLS389 3.2 29.4 1.0 C3 A:XLS389 3.2 30.8 1.0 CG A:ASP287 3.3 7.6 1.0 CD A:GLU217 3.3 6.9 1.0 OE1 A:GLU181 3.4 9.7 1.0 CG A:ASP245 3.5 9.1 1.0 C4 A:XLS389 3.6 29.9 1.0 O4 A:XLS389 3.6 30.0 1.0 CB A:ASP287 3.7 5.0 1.0 O A:HOH408 3.8 20.8 1.0 O A:HOH409 3.9 14.8 1.0 CB A:ASP245 4.0 5.0 1.0 CE1 A:HIS220 4.0 7.5 1.0 CG A:GLU217 4.0 5.0 1.0 CB A:GLU217 4.2 5.0 1.0 OE2 A:GLU217 4.2 14.0 1.0 OD1 A:ASP287 4.3 6.6 1.0 C2 A:XLS389 4.4 32.8 1.0 CG A:GLU181 4.4 7.7 1.0 OD1 A:ASP245 4.5 8.8 1.0 NE2 A:HIS220 4.6 11.5 1.0 O2 A:XLS389 4.8 34.0 1.0 ND1 A:HIS220 4.8 7.8 1.0 MN A:MN390 4.9 28.8 1.0

H.L.Carrell, H.Hoier, J.P.Glusker. Modes of Binding Substrates and Their Analogues to the Enzyme D-Xylose Isomerase. Acta Crystallogr.,Sect.D V. 50 113 1994.
ISSN: ISSN 0907-4449
PubMed: 15299449
DOI: 10.1107/S0907444993009345