Atomistry » Sodium » PDB 8piw-8qaw » 8pjd
Atomistry »
  Sodium »
    PDB 8piw-8qaw »
      8pjd »

Sodium in PDB 8pjd: Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445

Protein crystallography data

The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445, PDB code: 8pjd was solved by V.Cura, N.Troffer-Charlier, N.Marechal, L.Bonnefond, J.Cavarelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.25 / 1.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 65.052, 115.98, 133.718, 90, 90, 90
R / Rfree (%) 17.1 / 18.9

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445 (pdb code 8pjd). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445, PDB code: 8pjd:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 8pjd

Go back to Sodium Binding Sites List in 8pjd
Sodium binding site 1 out of 2 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na506

b:34.6
occ:1.00
OXT A:ACT504 2.5 28.4 1.0
O A:LYS383 2.6 24.4 1.0
HA A:GLN384 2.6 25.5 1.0
HA A:TRP354 2.7 26.5 1.0
OG1 A:THR373 2.8 20.8 1.0
HB A:THR373 2.9 26.2 1.0
HB2 A:TRP354 3.0 26.6 1.0
H1 A:ACT504 3.0 37.0 1.0
H2 A:ACT504 3.0 37.0 1.0
C A:ACT504 3.2 23.8 1.0
CH3 A:ACT504 3.2 30.9 1.0
HB3 A:TRP354 3.3 26.6 1.0
HG3 A:GLN384 3.3 29.1 1.0
CB A:THR373 3.3 21.9 1.0
HB3 A:TRP382 3.4 29.1 1.0
CB A:TRP354 3.4 22.2 1.0
CA A:TRP354 3.5 22.1 1.0
O A:THR373 3.5 23.0 1.0
C A:LYS383 3.5 23.5 1.0
CA A:GLN384 3.5 21.3 1.0
H A:PHE355 3.7 28.3 1.0
HB2 A:TRP382 3.8 29.1 1.0
N A:GLN384 3.9 23.5 1.0
O A:TRP382 4.0 23.7 1.0
O A:ALA353 4.0 20.9 1.0
CB A:TRP382 4.0 24.3 1.0
CG A:GLN384 4.2 24.3 1.0
HG21 A:THR373 4.2 26.6 1.0
H3 A:ACT504 4.2 37.0 1.0
C A:THR373 4.2 22.0 1.0
C A:TRP382 4.3 22.7 1.0
N A:PHE355 4.3 23.6 1.0
O A:ACT504 4.3 31.4 1.0
CB A:GLN384 4.4 22.9 1.0
NA A:NA507 4.4 27.5 1.0
CG2 A:THR373 4.4 22.2 1.0
H A:THR385 4.4 25.3 1.0
CA A:THR373 4.4 21.6 1.0
C A:TRP354 4.4 21.5 1.0
C A:GLN384 4.5 22.2 1.0
O A:HOH733 4.5 21.5 1.0
N A:TRP354 4.6 23.7 1.0
HB3 A:GLN384 4.6 27.4 1.0
N A:LYS383 4.6 21.5 1.0
HE21 A:GLN384 4.6 27.1 1.0
C A:ALA353 4.7 20.6 1.0
N A:THR385 4.7 21.1 1.0
CA A:LYS383 4.7 22.3 1.0
HG2 A:GLN384 4.7 29.1 1.0
H A:GLN384 4.8 28.2 1.0
HD2 A:PHE355 4.8 32.0 1.0
CG A:TRP354 4.8 20.6 1.0
CA A:TRP382 4.8 21.6 1.0
HG1 A:THR380 4.9 26.7 1.0
HA A:THR373 5.0 25.9 1.0
HG23 A:THR373 5.0 26.6 1.0

Sodium binding site 2 out of 2 in 8pjd

Go back to Sodium Binding Sites List in 8pjd
Sodium binding site 2 out of 2 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na507

b:27.5
occ:1.00
OXT A:ACT504 2.3 28.4 1.0
O A:TRP382 2.3 23.7 1.0
O A:SER302 2.4 26.2 1.0
O A:HOH834 2.5 29.5 1.0
OG1 A:THR385 2.5 29.8 1.0
HG1 A:THR385 2.9 35.7 1.0
C A:ACT504 3.1 23.8 1.0
HB2 A:SER302 3.2 31.9 1.0
O A:GLN384 3.2 25.0 1.0
O A:ACT504 3.3 31.4 1.0
HA A:SER302 3.3 28.5 1.0
C A:GLN384 3.4 22.2 1.0
C A:SER302 3.4 28.1 1.0
C A:TRP382 3.5 22.7 1.0
CA A:SER302 3.7 23.8 1.0
N A:THR385 3.8 21.1 1.0
HB3 A:TRP382 3.8 29.1 1.0
HA A:GLN384 3.8 25.5 1.0
HA A:THR385 3.8 25.3 1.0
CB A:THR385 3.8 24.4 1.0
CB A:SER302 3.9 26.6 1.0
N A:GLN384 3.9 23.5 1.0
HG23 A:THR227 3.9 31.2 1.0
CA A:GLN384 3.9 21.3 1.0
HB2 A:LYS383 4.0 30.4 1.0
CA A:THR385 4.0 21.1 1.0
HA A:TRP382 4.1 25.9 1.0
H A:GLN384 4.1 28.2 1.0
C A:LYS383 4.2 23.5 1.0
O A:HOH835 4.2 36.4 1.0
H A:THR385 4.2 25.3 1.0
CA A:TRP382 4.3 21.6 1.0
HB A:THR385 4.3 29.3 1.0
HA A:THR227 4.4 28.8 1.0
NA A:NA506 4.4 34.6 1.0
HB3 A:SER302 4.4 31.9 1.0
HA A:ASN303 4.5 31.5 1.0
CH3 A:ACT504 4.5 30.9 1.0
CB A:TRP382 4.5 24.3 1.0
N A:LYS383 4.5 21.5 1.0
N A:ASN303 4.6 26.0 1.0
O A:LYS383 4.6 24.4 1.0
H2 A:ACT504 4.7 37.0 1.0
CA A:LYS383 4.7 22.3 1.0
CB A:LYS383 4.7 25.3 1.0
HG23 A:THR385 4.7 31.3 1.0
H A:CYS228 4.8 28.5 1.0
CG2 A:THR385 4.8 26.1 1.0
H A:HIS304 4.8 28.5 1.0
CG2 A:THR227 4.8 26.0 1.0
HD1 A:TRP382 4.9 28.4 1.0
OG A:SER302 4.9 28.6 1.0
OG1 A:THR227 4.9 26.6 1.0

Reference:

V.Cura, N.Troffer-Charlier, N.Marechal, L.Bonnefond, J.Cavarelli. Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 94-445 To Be Published.
Page generated: Wed Oct 9 13:01:10 2024

Last articles

Zn in 2YRC
Zn in 2YQP
Zn in 2YR2
Zn in 2YQL
Zn in 2YPT
Zn in 2YPA
Zn in 2YPU
Zn in 2YNW
Zn in 2YNT
Zn in 2YNV
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy