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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: Tue Jul 30 01:04:46 2024

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