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Cobalt in PDB 5ul3: Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin Bound

Protein crystallography data

The structure of Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin Bound, PDB code: 5ul3 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) 49.80 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 89.357, 99.595, 121.439, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.2

Other elements in 5ul3:

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

Iron (Fe) 4 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin Bound (pdb code 5ul3). 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 Bound, PDB code: 5ul3:

Cobalt binding site 1 out of 1 in 5ul3

Go back to Cobalt Binding Sites List in 5ul3
Cobalt binding site 1 out of 1 in the Structure of Cobalamin-Dependent S-Adenosylmethionine Radical Enzyme Oxsb with Aqua-Cobalamin 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 Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co802

b:27.2
occ:1.00
CO A:B12802 0.0 27.2 1.0
N21 A:B12802 1.9 27.9 1.0
N24 A:B12802 1.9 23.7 1.0
N23 A:B12802 1.9 28.5 1.0
N22 A:B12802 1.9 29.5 1.0
O A:HOH1420 2.8 45.2 1.0
C19 A:B12802 2.8 25.9 1.0
C9 A:B12802 2.8 29.9 1.0
O A:HOH1396 2.8 39.4 1.0
C1 A:B12802 2.9 20.8 1.0
C11 A:B12802 2.9 32.8 1.0
C4 A:B12802 2.9 24.8 1.0
C16 A:B12802 3.0 25.3 1.0
C14 A:B12802 3.0 30.5 1.0
C6 A:B12802 3.0 25.4 1.0
C10 A:B12802 3.2 30.1 1.0
C5 A:B12802 3.4 29.0 1.0
C15 A:B12802 3.4 28.2 1.0
C20 A:B12802 3.5 26.5 1.0
O A:HOH1499 4.1 56.2 1.0
C18 A:B12802 4.1 20.7 1.0
C2 A:B12802 4.1 23.9 1.0
C12 A:B12802 4.2 34.4 1.0
C8 A:B12802 4.2 36.8 1.0
C3 A:B12802 4.2 25.4 1.0
C17 A:B12802 4.2 24.4 1.0
C7 A:B12802 4.3 30.8 1.0
C13 A:B12802 4.3 29.4 1.0
C26 A:B12802 4.5 22.8 1.0
O A:HOH1401 4.5 36.2 1.0
O A:HOH1004 4.6 34.6 1.0
C46 A:B12802 4.8 32.3 1.0
C35 A:B12802 4.8 28.3 1.0
O A:HOH1009 4.9 36.2 1.0
C54 A:B12802 4.9 22.0 1.0
C37 A:B12802 4.9 32.2 1.0
C48 A:B12802 4.9 32.6 1.0
C53 A:B12802 4.9 29.2 1.0
C41 A:B12802 4.9 36.0 1.0

Reference:

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
Page generated: Sun Jul 13 20:39:43 2025

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