Cobalt in PDB 5ul4: Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound

The structure of Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound, PDB code: 5ul4 was solved by J.Bridwell-Rabb, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.84 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.360, 99.600, 121.440, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 23.1

The structure of Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Cobalt atom in the Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound (pdb code 5ul4). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound, PDB code: 5ul4:

Cobalt binding site 1 out of 1 in the Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin and S-Adenosylmethionine Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Co802 b:40.0 occ:1.00 CO A:B12802 0.0 40.0 1.0 N21 A:B12802 1.9 40.0 1.0 N24 A:B12802 1.9 33.3 1.0 N23 A:B12802 1.9 33.6 1.0 N22 A:B12802 1.9 44.3 1.0 O A:HOH1017 2.5 45.0 1.0 O A:HOH1306 2.8 56.0 1.0 C9 A:B12802 2.8 43.6 1.0 C19 A:B12802 2.8 37.0 1.0 C1 A:B12802 2.9 35.4 1.0 C11 A:B12802 2.9 50.5 1.0 C4 A:B12802 2.9 35.8 1.0 C16 A:B12802 3.0 35.8 1.0 C14 A:B12802 3.0 46.1 1.0 C6 A:B12802 3.0 44.9 1.0 C10 A:B12802 3.2 42.7 1.0 C5 A:B12802 3.4 47.2 1.0 C15 A:B12802 3.4 39.2 1.0 C20 A:B12802 3.5 39.9 1.0 C18 A:B12802 4.1 28.2 1.0 C2 A:B12802 4.1 35.3 1.0 C12 A:B12802 4.2 50.1 1.0 C3 A:B12802 4.2 40.4 1.0 C8 A:B12802 4.2 47.9 1.0 O A:HOH1311 4.2 50.0 1.0 C17 A:B12802 4.2 32.9 1.0 C7 A:B12802 4.2 44.6 1.0 C13 A:B12802 4.3 49.0 1.0 O A:HOH912 4.4 43.0 0.5 C26 A:B12802 4.5 35.1 1.0 O A:HOH1379 4.5 61.0 1.0 O A:HOH917 4.6 46.0 1.0 C46 A:B12802 4.7 45.7 1.0 C37 A:B12802 4.8 46.3 1.0 C48 A:B12802 4.8 49.6 1.0 C54 A:B12802 4.8 29.6 1.0 C35 A:B12802 4.8 42.3 1.0 C53 A:B12802 4.9 36.5 1.0 C41 A:B12802 5.0 56.6 1.0

J.Bridwell-Rabb, A.Zhong, H.G.Sun, C.L.Drennan, H.W.Liu. A B12-Dependent Radical Sam Enzyme Involved in Oxetanocin A Biosynthesis. Nature V. 544 322 2017.
ISSN: ESSN 1476-4687
PubMed: 28346939
DOI: 10.1038/NATURE21689