Manganese in PDB 1xig: 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: 1xig 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)	14.00 / 1.70
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 1xig). 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: 1xig:
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:21.1 occ:0.80 OE2 A:GLU217 2.2 5.7 1.0 OD1 A:ASP257 2.4 7.5 1.0 O A:HOH409 2.5 6.1 1.0 OD2 A:ASP255 2.6 14.3 1.0 OD1 A:ASP255 2.6 17.1 1.0 NE2 A:HIS220 2.7 6.7 1.0 CG A:ASP255 2.9 15.7 1.0 CD A:GLU217 3.2 4.2 1.0 CD2 A:HIS220 3.2 3.2 1.0 CG A:ASP257 3.3 6.3 1.0 O1 A:XYL389 3.4 5.1 1.0 OD2 A:ASP257 3.5 12.3 1.0 OE1 A:GLU217 3.6 3.9 1.0 O2 A:XYL389 3.8 4.9 1.0 CE1 A:HIS220 3.9 4.7 1.0 ND2 A:ASN247 3.9 2.8 1.0 C1 A:XYL389 4.3 5.4 1.0 O A:HOH412 4.4 10.1 1.0 CB A:ASP255 4.4 10.7 1.0 CG A:GLU217 4.5 3.3 1.0 CG A:HIS220 4.5 3.5 1.0 C2 A:XYL389 4.6 4.5 1.0 NZ A:LYS183 4.7 7.7 1.0 CE A:LYS183 4.7 4.9 1.0 CB A:ASP257 4.7 4.3 1.0 ND1 A:HIS220 4.8 4.3 1.0 O A:HOH615 4.9 24.6 1.0 MN A:MN391 4.9 6.9 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:6.9 occ:1.00 OE1 A:GLU217 2.1 3.9 1.0 OE2 A:GLU181 2.2 2.5 1.0 OD2 A:ASP287 2.3 5.4 1.0 OD2 A:ASP245 2.3 5.0 1.0 O4 A:XYL389 2.3 5.4 1.0 O2 A:XYL389 2.3 4.9 1.0 CD A:GLU181 3.1 4.1 1.0 CD A:GLU217 3.2 4.2 1.0 CG A:ASP287 3.3 3.9 1.0 C4 A:XYL389 3.4 6.8 1.0 OE1 A:GLU181 3.4 3.2 1.0 CG A:ASP245 3.4 5.2 1.0 C2 A:XYL389 3.4 4.5 1.0 C3 A:XYL389 3.6 5.6 1.0 O3 A:XYL389 3.7 3.9 1.0 CB A:ASP287 3.7 4.7 1.0 CB A:ASP245 3.9 2.5 1.0 O A:HOH408 3.9 13.6 1.0 O A:HOH409 4.0 6.1 1.0 OE2 A:GLU217 4.1 5.7 1.0 CE1 A:HIS220 4.1 4.7 1.0 CG A:GLU217 4.2 3.3 1.0 CB A:GLU217 4.3 2.5 1.0 OD1 A:ASP287 4.3 4.6 1.0 OD1 A:ASP245 4.4 3.8 1.0 CG A:GLU181 4.4 2.5 1.0 NE2 A:HIS220 4.5 6.7 1.0 C5 A:XYL389 4.6 5.9 1.0 C1 A:XYL389 4.6 5.4 1.0 O1 A:XYL389 4.9 5.1 1.0 ND2 A:ASN215 4.9 2.6 1.0 MN A:MN390 4.9 21.1 0.8 ND1 A:HIS220 4.9 4.3 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