Manganese in PDB 2glk: High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution.

All present enzymatic activity of High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution.:
5.3.1.5;

The structure of High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution., PDB code: 2glk was solved by A.K.Katz, H.L.Carrell, B.L.Hanson, J.M.Harp, J.P.Glusker, G.J.Bunick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.36 / 0.94
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.712, 97.935, 101.867, 90.00, 90.00, 90.00
R / Rfree (%)	11.5 / 12.8

The binding sites of Manganese atom in the High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution. (pdb code 2glk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution., PDB code: 2glk:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn505 b:11.1 occ:0.50 OD2 A:ASP255 2.0 13.9 0.5 OE2 A:GLU217 2.1 16.1 1.0 OD1 A:ASP257 2.2 10.6 0.5 O A:HOH1316 2.2 22.3 1.0 OD1 A:ASP255 2.3 9.3 0.5 OD1 A:ASP255 2.5 20.1 0.5 CG A:ASP255 2.5 12.0 0.5 OD2 A:ASP255 2.7 14.8 0.5 NE2 A:HIS220 2.8 17.9 1.0 CG A:ASP255 2.8 19.2 0.5 CD A:GLU217 3.0 12.7 1.0 CG A:ASP257 3.1 9.3 0.5 OD1 A:ASP257 3.2 13.3 0.5 CD2 A:HIS220 3.2 13.4 1.0 OD2 A:ASP257 3.3 12.9 0.5 OE1 A:GLU217 3.3 18.7 1.0 O A:HOH1165 3.4 27.1 1.0 CG A:ASP257 3.8 9.5 0.5 OD2 A:ASP257 3.9 13.3 0.5 CE1 A:HIS220 3.9 19.0 1.0 ND2 A:ASN247 4.0 9.9 1.0 CB A:ASP255 4.0 15.7 1.0 O A:HOH1080 4.1 13.3 1.0 CG A:GLU217 4.4 8.5 1.0 CG A:HIS220 4.4 10.6 1.0 O A:HOH1121 4.5 22.2 1.0 NZ A:LYS183 4.6 14.2 1.0 CE A:LYS183 4.7 10.3 1.0 ND1 A:HIS220 4.8 14.4 1.0 CB A:ASP257 4.8 13.8 1.0 O A:HOH1203 4.8 42.5 1.0 CA A:ASP255 4.9 11.3 1.0

Manganese binding site 2 out of 2 in the High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of High-Resolution Study of D-Xylose Isomerase, 0.94A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn506 b:9.9 occ:0.50 OE2 A:GLU181 2.1 10.9 0.6 OD2 A:ASP287 2.2 15.5 1.0 OE1 A:GLU217 2.2 18.7 1.0 OD2 A:ASP245 2.3 17.2 1.0 O2 A:GOL601 2.4 13.6 1.0 O A:HOH1121 2.4 22.2 1.0 OE2 A:GLU181 2.8 11.7 0.4 CD A:GLU181 3.0 10.0 0.6 OE1 A:GLU181 3.2 11.3 0.4 CG A:ASP287 3.2 9.7 1.0 CD A:GLU181 3.3 9.3 0.4 C2 A:GOL601 3.4 15.0 1.0 CG A:ASP245 3.4 10.8 1.0 OE1 A:GLU181 3.4 10.1 0.6 CD A:GLU217 3.5 12.7 1.0 O1 A:GOL601 3.6 18.9 1.0 CB A:ASP287 3.6 8.9 1.0 O A:HOH1028 3.9 13.4 1.0 O A:HOH1316 3.9 22.3 1.0 CB A:ASP245 4.0 8.5 1.0 C1 A:GOL601 4.1 17.4 1.0 CE1 A:HIS220 4.1 19.0 1.0 CG A:GLU217 4.1 8.5 1.0 CB A:GLU217 4.2 8.1 1.0 OD1 A:ASP287 4.3 10.0 1.0 CG A:GLU181 4.4 9.7 0.6 OD1 A:ASP245 4.4 13.1 1.0 OE2 A:GLU217 4.4 16.1 1.0 CG A:GLU181 4.6 8.8 0.4 NE2 A:HIS220 4.6 17.9 1.0 C3 A:GOL601 4.7 14.1 1.0 ND2 A:ASN215 4.7 12.9 1.0 ND1 A:HIS220 4.9 14.4 1.0

A.K.Katz, X.Li, H.L.Carrell, B.L.Hanson, P.Langan, L.Coates, B.P.Schoenborn, J.P.Glusker, G.J.Bunick. Locating Active-Site Hydrogen Atoms in D-Xylose Isomerase: Time-of-Flight Neutron Diffraction. Proc.Natl.Acad.Sci.Usa V. 103 8342 2006.
ISSN: ISSN 0027-8424
PubMed: 16707576
DOI: 10.1073/PNAS.0602598103