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Cobalt in PDB 5t8y: Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site.

Enzymatic activity of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site.

All present enzymatic activity of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site.:
1.17.99.6;

Protein crystallography data

The structure of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site., PDB code: 5t8y was solved by D.P.Dowling, Z.D.Miles, C.Kohrer, S.J.Maiocco, S.J.Elliott, V.Bandarian, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.90 / 2.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.763, 111.030, 95.971, 90.00, 99.13, 90.00
R / Rfree (%) 23.8 / 26.7

Other elements in 5t8y:

The structure of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site. also contains other interesting chemical elements:

Iron (Fe) 16 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site. (pdb code 5t8y). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site., PDB code: 5t8y:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 5t8y

Go back to Cobalt Binding Sites List in 5t8y
Cobalt binding site 1 out of 2 in the Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site.


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co503

b:58.9
occ:1.00
CO A:B12503 0.0 58.9 1.0
N21 A:B12503 1.9 61.2 1.0
N24 A:B12503 1.9 60.1 1.0
N23 A:B12503 1.9 61.0 1.0
N22 A:B12503 1.9 60.5 1.0
C19 A:B12503 2.8 60.4 1.0
C4 A:B12503 2.9 61.0 1.0
C9 A:B12503 2.9 60.6 1.0
C1 A:B12503 2.9 60.6 1.0
C11 A:B12503 2.9 60.7 1.0
C14 A:B12503 2.9 60.5 1.0
C6 A:B12503 2.9 61.0 1.0
C16 A:B12503 3.0 60.8 1.0
C5 A:B12503 3.3 61.1 1.0
C10 A:B12503 3.3 60.4 1.0
C15 A:B12503 3.4 60.7 1.0
C20 A:B12503 3.5 60.4 1.0
C18 A:B12503 4.1 60.7 1.0
C2 A:B12503 4.2 61.2 1.0
C3 A:B12503 4.2 60.8 1.0
C49 A:B12503 4.2 60.0 1.0
C8 A:B12503 4.2 60.7 1.0
C7 A:B12503 4.2 60.8 1.0
C12 A:B12503 4.2 61.2 1.0
C13 A:B12503 4.2 61.0 1.0
C17 A:B12503 4.3 59.9 1.0
C35 A:B12503 4.7 60.8 1.0
C26 A:B12503 4.7 61.3 1.0
NH2 A:ARG141 4.8 61.7 1.0
C37 A:B12503 4.8 61.3 1.0
C48 A:B12503 4.8 61.2 1.0
C41 A:B12503 4.9 60.7 1.0
C46 A:B12503 4.9 61.1 1.0
C53 A:B12503 4.9 61.1 1.0

Cobalt binding site 2 out of 2 in 5t8y

Go back to Cobalt Binding Sites List in 5t8y
Cobalt binding site 2 out of 2 in the Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site.


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of Epoxyqueuosine Reductase From Bacillus Subtilis with the ASP134 Catalytic Loop Swung Out of the Active Site. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co503

b:66.6
occ:1.00
CO B:B12503 0.0 66.6 1.0
N21 B:B12503 1.9 69.5 1.0
N24 B:B12503 1.9 68.1 1.0
N23 B:B12503 1.9 68.7 1.0
N22 B:B12503 1.9 68.6 1.0
C19 B:B12503 2.8 68.5 1.0
C4 B:B12503 2.9 69.2 1.0
C1 B:B12503 2.9 68.7 1.0
C9 B:B12503 2.9 69.0 1.0
C11 B:B12503 2.9 67.9 1.0
C6 B:B12503 2.9 69.2 1.0
C14 B:B12503 2.9 68.5 1.0
C16 B:B12503 3.0 68.6 1.0
C5 B:B12503 3.3 68.7 1.0
C10 B:B12503 3.3 68.2 1.0
C15 B:B12503 3.4 68.7 1.0
C20 B:B12503 3.4 68.6 1.0
C18 B:B12503 4.1 68.7 1.0
C2 B:B12503 4.2 68.7 1.0
C3 B:B12503 4.2 68.7 1.0
C7 B:B12503 4.2 69.2 1.0
C8 B:B12503 4.2 68.6 1.0
C49 B:B12503 4.2 68.6 1.0
C12 B:B12503 4.2 68.8 1.0
C13 B:B12503 4.2 68.9 1.0
C17 B:B12503 4.3 68.0 1.0
NH2 B:ARG141 4.4 71.0 1.0
C35 B:B12503 4.7 68.5 1.0
C26 B:B12503 4.7 68.7 1.0
C37 B:B12503 4.7 68.4 1.0
C48 B:B12503 4.8 68.7 1.0
C46 B:B12503 4.9 69.0 1.0
C53 B:B12503 4.9 69.1 1.0
C41 B:B12503 4.9 69.9 1.0
C30 B:B12503 5.0 69.5 1.0

Reference:

D.P.Dowling, Z.D.Miles, C.Kohrer, S.J.Maiocco, S.J.Elliott, V.Bandarian, C.L.Drennan. Molecular Basis of Cobalamin-Dependent Rna Modification. Nucleic Acids Res. V. 44 9965 2016.
ISSN: ESSN 1362-4962
PubMed: 27638883
DOI: 10.1093/NAR/GKW806
Page generated: Sun Jul 13 20:37:55 2025

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