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Atomistry » Manganese » PDB 5svc-5uqn » 5udr | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 5svc-5uqn » 5udr » |
Manganese in PDB 5udr: Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase in Complex with Nicotinamide Mononucleotid NmnProtein crystallography data
The structure of Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase in Complex with Nicotinamide Mononucleotid Nmn, PDB code: 5udr
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:
Manganese Binding Sites:
The binding sites of Manganese atom in the Lare, A Sulfur Transferase Involved in Synthesis of the Cofactor For Lactate Racemase in Complex with Nicotinamide Mononucleotid Nmn
(pdb code 5udr). 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 Nicotinamide Mononucleotid Nmn, PDB code: 5udr: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 5udrGo back to Manganese Binding Sites List in 5udr
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 Nicotinamide Mononucleotid Nmn
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 5udrGo back to Manganese Binding Sites List in 5udr
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 Nicotinamide Mononucleotid Nmn
Mono view Stereo pair view
Reference:
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..
Page generated: Tue Dec 15 04:47:06 2020
ISSN: ESSN 1091-6490 PubMed: 28784764 DOI: 10.1073/PNAS.1704967114 |
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