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Sodium in PDB 6hon: Drosophila NOT4 Cbm Peptide Bound to Human CAF40

Protein crystallography data

The structure of Drosophila NOT4 Cbm Peptide Bound to Human CAF40, PDB code: 6hon was solved by T.Raisch, E.Izaurralde, O.Weichenrieder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.25 / 2.20
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.630, 90.320, 196.990, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23

Other elements in 6hon:

The structure of Drosophila NOT4 Cbm Peptide Bound to Human CAF40 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Drosophila NOT4 Cbm Peptide Bound to Human CAF40 (pdb code 6hon). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Drosophila NOT4 Cbm Peptide Bound to Human CAF40, PDB code: 6hon:

Sodium binding site 1 out of 1 in 6hon

Go back to Sodium Binding Sites List in 6hon
Sodium binding site 1 out of 1 in the Drosophila NOT4 Cbm Peptide Bound to Human CAF40


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Drosophila NOT4 Cbm Peptide Bound to Human CAF40 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:73.4
occ:0.50
OE1 A:GLN201 2.8 0.8 1.0
O A:HOH420 3.0 67.4 1.0
CD A:GLN201 3.7 0.8 1.0
O A:ALA197 3.9 67.8 1.0
CA A:TYR198 3.9 60.0 1.0
CG A:GLN201 4.0 81.8 1.0
C A:ALA197 4.1 66.4 1.0
N A:TYR198 4.1 61.9 1.0
CB A:GLN201 4.1 67.4 1.0
CB A:ALA197 4.5 63.8 1.0
CB A:TYR198 4.7 60.8 1.0
NH2 A:ARG205 4.8 69.5 1.0
O A:HOH436 4.8 66.9 1.0
NE2 A:GLN201 4.9 93.1 1.0
CA A:ALA197 5.0 62.6 1.0

Reference:

C.Keskeny, T.Raisch, A.Sgromo, C.Igreja, D.Bhandari, O.Weichenrieder, E.Izaurralde. A Conserved CAF40-Binding Motif in Metazoan NOT4 Mediates Association with the CCR4-Not Complex. Genes Dev. V. 33 236 2019.
ISSN: ISSN 1549-5477
PubMed: 30692204
DOI: 10.1101/GAD.320952.118
Page generated: Tue Oct 8 09:23:15 2024

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