Atomistry » Chlorine » PDB 5fs0-5fza » 5fwa
Atomistry »
  Chlorine »
    PDB 5fs0-5fza »
      5fwa »

Chlorine in PDB 5fwa: Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1

Enzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1

All present enzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1:
2.1.1.125;

Protein crystallography data

The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1, PDB code: 5fwa 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) 43.37 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.183, 114.676, 132.653, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.1

Other elements in 5fwa:

The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1 (pdb code 5fwa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1, PDB code: 5fwa:

Chlorine binding site 1 out of 1 in 5fwa

Go back to Chlorine Binding Sites List in 5fwa
Chlorine binding site 1 out of 1 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1448

b:40.7
occ:1.00
 O A:HOH2132 3.2 52.8 1.0
ND1 A:HIS377 3.2 41.3 1.0
N A:LEU376 3.3 31.9 1.0
CB A:LEU376 3.5 36.4 1.0
CD A:PRO375 3.5 28.2 1.0
CE1 A:HIS377 3.5 38.6 1.0
CA A:GLY374 3.5 26.4 1.0
N A:PRO375 3.6 28.3 1.0
C A:GLY374 3.6 28.0 1.0
O A:HOH2230 3.6 57.3 1.0
CA A:LEU376 3.9 33.5 1.0
CG A:LEU376 4.0 41.7 1.0
CG A:PRO375 4.1 32.9 1.0
O A:GLY374 4.3 27.6 1.0
CZ2 A:TRP354 4.3 31.5 1.0
C A:PRO375 4.3 33.9 1.0
NE1 A:TRP354 4.3 26.5 1.0
CD1 A:LEU376 4.4 44.5 1.0
N A:HIS377 4.4 28.1 1.0
CE2 A:TRP354 4.5 27.9 1.0
CA A:PRO375 4.5 29.5 1.0
C A:LEU376 4.5 35.4 1.0
N A:GLY374 4.5 26.2 1.0
CG A:HIS377 4.5 36.6 1.0
OG A:SER372 4.6 35.5 1.0
O A:HOH2199 4.7 60.6 1.0
NE2 A:HIS377 4.8 40.6 1.0
CB A:PRO375 4.9 31.7 1.0

Reference:

V.Cura, N.Marechal, N.Troffer-Charlier, J.M.Strub, M.J.Van Haren, N.I.Martin, S.Cianferani, L.Bonnefond, J.Cavarelli. Structural Studies of Protein Arginine Methyltransferase 2 Reveal Its Interactions with Potential Substrates and Inhibitors. Febs J. V. 284 77 2017.
ISSN: ISSN 1742-4658
PubMed: 27879050
DOI: 10.1111/FEBS.13953
Page generated: Fri Jul 26 08:12:25 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy