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Potassium in PDB 3f4e: Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna.

Protein crystallography data

The structure of Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna., PDB code: 3f4e was solved by A.A.Serganov, L.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.05
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.471, 71.471, 140.554, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 23.2

Other elements in 3f4e:

The structure of Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna. also contains other interesting chemical elements:

Magnesium (Mg) 13 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna. (pdb code 3f4e). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna., PDB code: 3f4e:

Potassium binding site 1 out of 1 in 3f4e

Go back to Potassium Binding Sites List in 3f4e
Potassium binding site 1 out of 1 in the Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Fmn Riboswitch Bound to Fmn, Split Rna. within 5.0Å range:
probe atom residue distance (Å) B Occ
X:K300

b:98.4
occ:1.00
O4 X:U37 3.8 74.3 1.0
O6 X:G36 3.9 65.0 1.0
O6 X:G35 3.9 67.2 1.0
N7 X:G36 4.2 66.6 1.0
C2' X:A40 4.2 64.3 1.0
OP2 X:A40 4.2 65.6 1.0
N7 X:G35 4.3 67.5 1.0
O2' X:A40 4.3 64.7 1.0
C6 X:G35 4.6 66.8 1.0
C6 X:G36 4.7 66.3 1.0
C5 X:G35 4.8 66.5 1.0
C5 X:G36 4.8 66.4 1.0
C8 X:A40 4.9 64.6 1.0
C4 X:U37 4.9 74.0 1.0
C3' X:A40 5.0 64.8 1.0

Reference:

A.Serganov, L.Huang, D.J.Patel. Coenzyme Recognition and Gene Regulation By A Flavin Mononucleotide Riboswitch. Nature V. 458 233 2009.
ISSN: ISSN 0028-0836
PubMed: 19169240
DOI: 10.1038/NATURE07642
Page generated: Sun Dec 13 23:18:19 2020

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