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Atomistry » Manganese » PDB 6bh5-6dk4 » 6btd » |
Manganese in PDB 6btd: Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-DeoxyriboseEnzymatic activity of Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose
All present enzymatic activity of Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose:
4.1.2.17; Protein crystallography data
The structure of Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose, PDB code: 6btd
was solved by
Q.Li,
S.D.Bruner,
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 Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose
(pdb code 6btd). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose, PDB code: 6btd: Manganese binding site 1 out of 1 in 6btdGo back to Manganese Binding Sites List in 6btd
Manganese binding site 1 out
of 1 in the Crystal Structure of Deoxyribose-Phosphate Aldolase From Bacillus Thuringiensis Involved in Dispatching the Ubiquitous Radical Sam Enzyme Byproduct 5-Deoxyribose
Mono view Stereo pair view
Reference:
G.A.W.Beaudoin,
Q.Li,
J.Folz,
O.Fiehn,
J.L.Goodsell,
A.Angerhofer,
S.D.Bruner,
A.D.Hanson.
Salvage of the 5-Deoxyribose Byproduct of Radical Sam Enzymes. Nat Commun V. 9 3105 2018.
Page generated: Tue Dec 15 04:51:06 2020
ISSN: ESSN 2041-1723 PubMed: 30082730 DOI: 10.1038/S41467-018-05589-4 |
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