Manganese in PDB 5udu: Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese

The structure of Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese, PDB code: 5udu was solved by M.Fellner, B.Desguin, R.P.Hausinger, J.Hu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.28 / 2.79
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.949, 107.949, 320.406, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25

The binding sites of Manganese atom in the Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese (pdb code 5udu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese, PDB code: 5udu:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:84.1 occ:1.00 O B:HOH404 2.0 89.7 1.0 OD2 B:ASP231 2.1 0.1 1.0 OD2 A:ASP231 2.1 97.8 1.0 OD1 A:ASP231 2.1 0.0 1.0 OD2 C:ASP231 2.2 0.9 1.0 OD1 C:ASP231 2.2 0.8 1.0 OD1 B:ASP231 2.2 0.9 1.0 CG A:ASP231 2.4 85.1 1.0 CG B:ASP231 2.5 99.6 1.0 CG C:ASP231 2.5 99.0 1.0 CB A:ASP231 4.0 61.3 1.0 CB C:ASP231 4.0 71.8 1.0 CB B:ASP231 4.0 78.0 1.0 O B:HOH402 4.4 49.6 1.0 O B:ALA227 4.8 42.8 1.0 CA A:ASP231 4.8 52.8 1.0 CA C:ASP231 4.8 58.1 1.0 CA B:ASP231 4.9 59.5 1.0 O C:ALA227 4.9 59.0 1.0 N C:ASP231 4.9 53.4 1.0 N A:ASP231 4.9 55.7 1.0 N B:ASP231 5.0 55.4 1.0 O A:ALA227 5.0 40.0 1.0

Manganese binding site 2 out of 2 in the Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase, in Complex with Manganese within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn301 b:63.0 occ:0.81 OD2 D:ASP231 2.1 81.9 1.0 OD2 E:ASP231 2.2 0.3 1.0 OD1 F:ASP231 2.2 0.7 1.0 OD1 D:ASP231 2.2 86.0 1.0 OD2 F:ASP231 2.2 97.8 1.0 OD1 E:ASP231 2.2 94.5 1.0 O F:HOH404 2.3 54.4 1.0 CG D:ASP231 2.4 73.5 1.0 CG F:ASP231 2.5 87.1 1.0 CG E:ASP231 2.5 83.5 1.0 CB D:ASP231 4.0 61.6 1.0 CB F:ASP231 4.0 74.2 1.0 CB E:ASP231 4.0 45.9 1.0 O D:ALA227 4.6 39.3 1.0 CA F:ASP231 4.8 67.5 1.0 CA D:ASP231 4.8 56.3 1.0 CA E:ASP231 4.8 44.7 1.0 O E:ALA227 4.9 81.7 1.0 N D:ASP231 4.9 53.5 1.0 N F:ASP231 4.9 68.0 1.0 N E:ASP231 4.9 58.0 1.0

M.Fellner, B.Desguin, R.P.Hausinger, J.Hu. Structural Insights Into the Catalytic Mechanism of A Sacrificial Sulfur Insertase of the N-Type Atp Pyrophosphatase Family, Lare. Proc. Natl. Acad. Sci. V. 114 9074 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28784764
DOI: 10.1073/PNAS.1704967114