Manganese in PDB 8jqe: Structure of Cmcbda in Complex with MN2+ and Glycerol

The structure of Structure of Cmcbda in Complex with MN2+ and Glycerol, PDB code: 8jqe was solved by X.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.99 / 2.31
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.617, 60.27, 87.444, 90, 111.11, 90
R / Rfree (%)	16 / 21.4

The binding sites of Manganese atom in the Structure of Cmcbda in Complex with MN2+ and Glycerol (pdb code 8jqe). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Cmcbda in Complex with MN2+ and Glycerol, PDB code: 8jqe:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Cmcbda in Complex with MN2+ and Glycerol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Cmcbda in Complex with MN2+ and Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:39.0 occ:1.00 OD1 A:ASP22 2.1 38.9 1.0 ND1 A:HIS143 2.2 38.4 1.0 O1 A:PO4403 2.3 40.4 1.0 NE2 A:HIS72 2.3 43.7 1.0 O2 A:PO4403 2.6 50.9 1.0 O1 A:GOL401 2.8 51.2 1.0 CE1 A:HIS143 3.0 39.5 1.0 P A:PO4403 3.0 47.1 1.0 CG A:ASP22 3.1 35.5 1.0 CE1 A:HIS72 3.2 38.9 1.0 CD2 A:HIS72 3.3 37.5 1.0 OD2 A:ASP22 3.3 34.6 1.0 CG A:HIS143 3.4 41.4 1.0 C1 A:GOL401 3.7 48.2 1.0 CA A:HIS143 3.7 36.9 1.0 CB A:HIS143 3.9 35.8 1.0 O3 A:PO4403 3.9 58.2 1.0 CB A:ASP21 4.0 39.4 1.0 NE2 A:HIS230 4.0 46.2 1.0 N A:MET144 4.1 40.3 1.0 NE2 A:HIS143 4.2 41.0 1.0 O4 A:PO4403 4.2 64.6 1.0 CD2 A:HIS230 4.2 37.6 1.0 ND1 A:HIS72 4.4 43.7 1.0 CD2 A:HIS143 4.4 41.4 1.0 OD2 A:ASP21 4.4 52.2 1.0 CG A:HIS72 4.4 35.9 1.0 CB A:ASP22 4.5 32.0 1.0 C A:HIS143 4.5 38.6 1.0 N A:ASP22 4.5 38.0 1.0 CG A:ASP21 4.6 48.8 1.0 CA A:ASP22 4.8 36.0 1.0 N A:HIS143 4.8 37.7 1.0 SD A:MET48 4.9 41.8 1.0 C2 A:GOL401 4.9 56.5 1.0 O2 A:GOL401 5.0 51.5 1.0

Manganese binding site 2 out of 2 in the Structure of Cmcbda in Complex with MN2+ and Glycerol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Cmcbda in Complex with MN2+ and Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn402 b:26.2 occ:1.00 OD1 B:ASP22 2.1 25.7 1.0 O4 B:PO4403 2.2 29.9 1.0 ND1 B:HIS143 2.3 26.0 1.0 NE2 B:HIS72 2.3 30.7 1.0 O3 B:GOL401 2.3 34.8 1.0 O2 B:PO4403 2.8 31.1 1.0 P B:PO4403 3.0 31.7 1.0 CE1 B:HIS143 3.1 26.0 1.0 CD2 B:HIS72 3.2 23.5 1.0 CG B:ASP22 3.2 32.9 1.0 CG B:HIS143 3.4 34.4 1.0 C3 B:GOL401 3.4 35.1 1.0 CE1 B:HIS72 3.4 29.2 1.0 OD2 B:ASP22 3.6 33.4 1.0 CA B:HIS143 3.7 31.1 1.0 CB B:HIS143 3.8 24.5 1.0 O1 B:PO4403 4.0 35.5 1.0 N B:MET144 4.1 30.8 1.0 O3 B:PO4403 4.1 32.3 1.0 CB B:ASP21 4.2 30.7 1.0 NE2 B:HIS143 4.3 33.4 1.0 NE2 B:HIS230 4.4 32.0 1.0 CG B:HIS72 4.4 29.4 1.0 C2 B:GOL401 4.4 38.9 1.0 CD2 B:HIS143 4.4 24.7 1.0 ND1 B:HIS72 4.5 32.5 1.0 C B:HIS143 4.5 32.4 1.0 CD2 B:HIS230 4.5 25.4 1.0 N B:ASP22 4.5 27.2 1.0 CB B:ASP22 4.5 24.9 1.0 OD2 B:ASP21 4.6 39.5 1.0 CA B:ASP22 4.8 25.4 1.0 N B:HIS143 4.8 28.8 1.0 O2 B:GOL401 4.9 39.3 1.0 CG B:ASP21 4.9 34.0 1.0 SD B:MET48 4.9 34.0 1.0 CE B:MET48 5.0 23.7 1.0

S.Hu, L.Xu, C.Xie, J.Hong. Structural Insights Into the Catalytic Activity of Cyclobacterium Marinum N -Acetylglucosamine Deacetylase. J.Agric.Food Chem. 2023.
ISSN: ESSN 1520-5118
PubMed: 38141024
DOI: 10.1021/ACS.JAFC.3C06146