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Potassium in PDB 5de8: Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form.

Protein crystallography data

The structure of Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form., PDB code: 5de8 was solved by N.Vasilyev, A.Polonskaia, J.C.Darnell, R.B.Darnell, D.J.Patel, A.Serganov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.36 / 3.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 57.650, 130.600, 36.700, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 22.7

Other elements in 5de8:

The structure of Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form. also contains other interesting chemical elements:

Iridium (Ir) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form. (pdb code 5de8). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form., PDB code: 5de8:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 5de8

Go back to Potassium Binding Sites List in 5de8
Potassium binding site 1 out of 2 in the Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form.


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 Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K101

b:28.0
occ:0.71
O6 A:G12 2.5 47.6 1.0
O6 A:G24 2.5 15.5 1.0
O6 A:G15 2.6 22.3 1.0
O6 A:G11 2.7 38.4 1.0
O6 A:G25 2.7 17.9 1.0
O6 A:G20 2.9 20.6 1.0
O6 A:G16 3.0 21.9 1.0
O6 A:G21 3.2 21.3 1.0
C6 A:G12 3.4 33.5 1.0
C6 A:G24 3.4 18.4 1.0
C6 A:G25 3.5 33.0 1.0
N1 A:G25 3.6 42.8 1.0
N1 A:G24 3.6 18.3 1.0
C6 A:G15 3.7 23.8 1.0
C6 A:G11 3.7 24.6 1.0
N1 A:G12 3.8 49.6 1.0
C6 A:G20 3.8 20.1 1.0
N1 A:G20 4.0 39.3 1.0
N1 A:G11 4.0 29.8 1.0
C6 A:G21 4.0 18.8 1.0
C6 A:G16 4.1 20.3 1.0
N1 A:G21 4.1 19.0 1.0
N1 A:G15 4.2 21.5 1.0
C5 A:G12 4.5 36.0 1.0
N1 A:G16 4.5 19.5 1.0
C5 A:G24 4.7 29.1 1.0
C2 A:G25 4.8 14.7 1.0
C5 A:G25 4.8 33.4 1.0
C5 A:G15 4.9 28.1 1.0
C2 A:G24 4.9 16.7 1.0

Potassium binding site 2 out of 2 in 5de8

Go back to Potassium Binding Sites List in 5de8
Potassium binding site 2 out of 2 in the Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Complex Between Human Fmrp Rgg Motif and G- Quadruplex Rna, Iridium Hexammine Bound Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K101

b:65.6
occ:1.00
O6 C:G20 2.6 66.4 1.0
O6 C:G15 2.7 35.2 1.0
O6 C:G16 2.7 34.6 1.0
O6 C:G11 2.7 37.5 1.0
O6 C:G12 2.8 42.4 1.0
O6 C:G24 2.9 56.9 1.0
O6 C:G21 3.0 54.4 1.0
O6 C:G25 3.2 45.4 1.0
C6 C:G20 3.5 50.7 1.0
C6 C:G16 3.6 34.2 1.0
C6 C:G11 3.6 51.3 1.0
C6 C:G12 3.6 41.5 1.0
C6 C:G15 3.7 34.7 1.0
N1 C:G11 3.7 47.4 1.0
C6 C:G24 3.7 53.4 1.0
N1 C:G24 3.7 53.2 1.0
C6 C:G21 3.8 52.8 1.0
N1 C:G16 3.8 44.2 1.0
N1 C:G20 3.8 52.0 1.0
C6 C:G25 3.9 49.9 1.0
N1 C:G21 4.0 60.1 1.0
N1 C:G12 4.0 50.6 1.0
N1 C:G25 4.0 44.9 1.0
N1 C:G15 4.1 34.4 1.0
C5 C:G20 4.8 35.8 1.0
C5 C:G12 4.8 42.0 1.0
C5 C:G15 4.9 47.0 1.0
C5 C:G16 4.9 33.9 1.0
O6 C:G6 5.0 57.5 1.0
C5 C:G11 5.0 49.3 1.0

Reference:

N.Vasilyev, A.Polonskaia, J.C.Darnell, R.B.Darnell, D.J.Patel, A.Serganov. Crystal Structure Reveals Specific Recognition of A G-Quadruplex Rna By A Beta-Turn in the Rgg Motif of Fmrp. Proc.Natl.Acad.Sci.Usa V. 112 E5391 2015.
ISSN: ESSN 1091-6490
PubMed: 26374839
DOI: 10.1073/PNAS.1515737112
Page generated: Sun Dec 13 23:56:19 2020

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