Atomistry » Chlorine » PDB 7nou-7nwa » 7nqq
Atomistry »
  Chlorine »
    PDB 7nou-7nwa »
      7nqq »

Chlorine in PDB 7nqq: Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2

Enzymatic activity of Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2

All present enzymatic activity of Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2:
2.7.11.24;

Protein crystallography data

The structure of Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2, PDB code: 7nqq was solved by M.O'reilly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.53 / 1.94
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.94, 70.684, 60.927, 90, 109.86, 90
R / Rfree (%) 17.5 / 22.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2 (pdb code 7nqq). 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 Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2, PDB code: 7nqq:

Chlorine binding site 1 out of 1 in 7nqq

Go back to Chlorine Binding Sites List in 7nqq
Chlorine binding site 1 out of 1 in the Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:30.6
occ:1.00
 CL39 A:UMN406 0.0 30.6 1.0
C38 A:UMN406 1.7 29.9 1.0
H58 A:UMN406 2.7 32.4 1.0
C37 A:UMN406 2.7 29.4 1.0
C26 A:UMN406 2.7 30.3 1.0
H69 A:UMN406 2.8 29.4 1.0
OE1 A:GLN105 3.0 28.1 1.0
C22 A:UMN406 3.1 32.4 1.0
C21 A:UMN406 3.1 31.5 1.0
CD A:GLN105 3.5 29.7 1.0
CB A:GLN105 3.7 32.1 1.0
O A:HOH659 3.8 42.1 1.0
N36 A:UMN406 4.0 29.4 1.0
N27 A:UMN406 4.0 30.0 1.0
CB A:ALA52 4.1 37.3 1.0
CG A:GLN105 4.2 30.2 1.0
NE2 A:GLN105 4.2 29.4 1.0
C23 A:UMN406 4.2 33.7 1.0
CG1 A:ILE84 4.2 27.7 1.0
CD1 A:LEU156 4.2 27.2 1.0
C20 A:UMN406 4.3 32.5 1.0
O A:ASP106 4.3 33.9 1.0
C28 A:UMN406 4.4 30.6 1.0
CD1 A:ILE84 4.4 30.2 1.0
H57 A:UMN406 4.7 32.5 1.0
NZ A:LYS54 5.0 36.6 1.0
CA A:GLN105 5.0 31.1 1.0

Reference:

T.D.Heightman, V.Berdini, L.Bevan, I.M.Buck, M.G.Carr, A.Courtin, J.E.Coyle, J.E.H.Day, C.East, L.Fazal, C.M.Griffiths-Jones, S.Howard, J.Kucia-Tran, V.Martins, S.Muench, J.M.Munck, D.Norton, M.O'reilly, N.Palmer, P.Pathuri, T.M.Peakman, M.Reader, D.C.Rees, S.J.Rich, A.Shah, N.G.Wallis, H.Walton, N.E.Wilsher, A.J.Woolford, M.Cooke, D.Cousin, S.Onions, J.Shannon, J.Watts, C.W.Murray. Discovery of ASTX029, A Clinical Candidate Which Modulates the Phosphorylation and Catalytic Activity of ERK1/2. J.Med.Chem. V. 64 12286 2021.
ISSN: ISSN 0022-2623
PubMed: 34387469
DOI: 10.1021/ACS.JMEDCHEM.1C00905
Page generated: Sun Jul 13 04:32:42 2025

Last articles

Fe in 2C2F
Fe in 2C2C
Fe in 2C2U
Fe in 2C2J
Fe in 2C1D
Fe in 2C1U
Fe in 2C1V
Fe in 2BW1
Fe in 2C0K
Fe in 2BZ9
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy