Manganese in PDB 1xif: 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: 1xif 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)	10.00 / 1.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.860, 99.530, 103.080, 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 1xif). 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: 1xif:
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:4.3 occ:1.00 OE2 A:GLU217 2.1 4.0 1.0 OD1 A:ASP257 2.3 2.6 1.0 O A:HOH409 2.3 2.5 1.0 OD2 A:ASP255 2.3 3.1 1.0 NE2 A:HIS220 2.4 3.1 1.0 OD1 A:ASP255 2.4 2.5 1.0 CG A:ASP255 2.7 3.7 1.0 CD A:GLU217 3.0 3.3 1.0 OE1 A:GLU217 3.0 2.5 1.0 CD2 A:HIS220 3.0 2.5 1.0 CG A:ASP257 3.2 4.5 1.0 OD2 A:ASP257 3.4 5.4 1.0 CE1 A:HIS220 3.4 4.1 1.0 O A:HOH565 3.8 6.3 1.0 ND2 A:ASN247 4.0 2.5 1.0 O A:HOH412 4.0 3.6 1.0 O3 A:GLC389 4.1 4.1 1.0 CG A:HIS220 4.2 2.5 1.0 CB A:ASP255 4.2 2.5 1.0 OD2 A:ASP287 4.4 7.5 1.0 ND1 A:HIS220 4.4 3.0 1.0 CG A:GLU217 4.4 2.5 1.0 CB A:ASP257 4.6 2.5 1.0 MN A:MN391 4.6 5.5 1.0 O A:HOH615 4.8 20.2 1.0 CA A:ASP257 5.0 2.5 1.0 N A:ASP257 5.0 2.5 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:5.5 occ:1.00 OE1 A:GLU217 2.2 2.5 1.0 OE2 A:GLU181 2.2 4.1 1.0 OD2 A:ASP245 2.2 4.5 1.0 OD2 A:ASP287 2.2 7.5 1.0 O4 A:GLC389 2.3 6.2 1.0 O3 A:GLC389 2.5 4.1 1.0 CD A:GLU181 3.1 5.2 1.0 C4 A:GLC389 3.1 9.3 1.0 C3 A:GLC389 3.1 7.8 1.0 CG A:ASP287 3.3 6.2 1.0 CD A:GLU217 3.3 3.3 1.0 CG A:ASP245 3.4 5.8 1.0 OE1 A:GLU181 3.4 5.8 1.0 CB A:ASP287 3.7 3.9 1.0 O A:HOH409 3.8 2.5 1.0 CB A:ASP245 4.0 2.5 1.0 CE1 A:HIS220 4.0 4.1 1.0 CG A:GLU217 4.1 2.5 1.0 O A:HOH408 4.1 13.2 1.0 CB A:GLU217 4.2 2.5 1.0 OE2 A:GLU217 4.3 4.0 1.0 OD1 A:ASP245 4.3 4.5 1.0 OD1 A:ASP287 4.3 5.5 1.0 CG A:GLU181 4.4 3.6 1.0 C5 A:GLC389 4.4 12.3 1.0 NE2 A:HIS220 4.6 3.1 1.0 C2 A:GLC389 4.6 9.2 1.0 MN A:MN390 4.6 4.3 1.0 ND1 A:HIS220 4.7 3.0 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