Manganese in PDB 5zyc: Crystal Structure of Glucose Isomerase Soaked with MN2+

All present enzymatic activity of Crystal Structure of Glucose Isomerase Soaked with MN2+:
5.3.1.5;

The structure of Crystal Structure of Glucose Isomerase Soaked with MN2+, PDB code: 5zyc was solved by K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.63 / 1.75
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.456, 97.921, 101.988, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 18.4

The binding sites of Manganese atom in the Crystal Structure of Glucose Isomerase Soaked with MN2+ (pdb code 5zyc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Glucose Isomerase Soaked with MN2+, PDB code: 5zyc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Glucose Isomerase Soaked with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Glucose Isomerase Soaked with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:18.9 occ:1.00 O A:HOH501 1.7 17.9 1.0 OE1 A:GLU217 2.1 12.6 1.0 OD1 A:ASP257 2.2 16.3 1.0 OD2 A:ASP255 2.2 20.2 1.0 OD1 A:ASP255 2.3 17.6 1.0 O A:HOH559 2.3 20.9 1.0 NE2 A:HIS220 2.6 11.6 1.0 CG A:ASP255 2.6 19.3 1.0 CD A:GLU217 3.1 11.7 1.0 CD2 A:HIS220 3.2 9.2 1.0 CG A:ASP257 3.2 15.1 1.0 OD2 A:ASP257 3.4 20.1 1.0 OE2 A:GLU217 3.5 14.2 1.0 O A:HOH767 3.6 18.3 1.0 CE1 A:HIS220 3.7 11.8 1.0 O A:HOH674 3.9 23.8 1.0 ND2 A:ASN247 4.0 9.2 1.0 CB A:ASP255 4.1 14.2 1.0 O A:HOH601 4.3 11.8 1.0 CG A:GLU217 4.4 9.2 1.0 CG A:HIS220 4.4 9.0 1.0 NZ A:LYS183 4.5 14.4 1.0 CE A:LYS183 4.6 11.8 1.0 CB A:ASP257 4.6 11.7 1.0 ND1 A:HIS220 4.7 10.5 1.0 OD2 A:ASP287 4.8 14.5 1.0 O A:HOH692 5.0 35.5 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Glucose Isomerase Soaked with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Glucose Isomerase Soaked with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:11.7 occ:1.00 OE2 A:GLU181 2.1 9.8 1.0 OD2 A:ASP287 2.1 14.5 1.0 OE2 A:GLU217 2.1 14.2 1.0 OD2 A:ASP245 2.1 10.0 1.0 O2 A:EDO404 2.3 14.8 1.0 O A:HOH674 2.5 23.8 1.0 CD A:GLU181 3.0 11.7 1.0 CG A:ASP287 3.2 10.6 1.0 CG A:ASP245 3.2 9.5 1.0 C2 A:EDO404 3.2 17.2 1.0 OE1 A:GLU181 3.2 11.2 1.0 CD A:GLU217 3.3 11.7 1.0 CB A:ASP287 3.6 10.2 1.0 O A:HOH501 3.7 17.9 1.0 CB A:ASP245 3.8 9.6 1.0 O A:HOH723 4.0 16.3 1.0 O A:HOH559 4.2 20.9 1.0 CE1 A:HIS220 4.2 11.8 1.0 OD1 A:ASP245 4.2 9.9 1.0 CG A:GLU217 4.2 9.2 1.0 OE1 A:GLU217 4.2 12.6 1.0 CB A:GLU217 4.3 8.5 1.0 OD1 A:ASP287 4.3 9.8 1.0 CG A:GLU181 4.3 10.7 1.0 ND2 A:ASN215 4.5 9.2 1.0 C1 A:EDO404 4.6 16.9 1.0 NE2 A:HIS220 4.7 11.6 1.0 O A:HOH767 4.9 18.3 1.0 ND1 A:HIS220 5.0 10.5 1.0

J.E.Bae, K.Y.Hwang, K.H.Nam. Structural Analysis of Substrate Recognition By Glucose Isomerase in MN2+Binding Mode at M2 Site in S. Rubiginosus Biochem. Biophys. Res. V. 503 770 2018COMMUN..
ISSN: ESSN 1090-2104
PubMed: 29909012
DOI: 10.1016/J.BBRC.2018.06.074