Chlorine in PDB 7pqk: Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate

Enzymatic activity of Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate

All present enzymatic activity of Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate:
6.1.1.4;

Protein crystallography data

The structure of Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate, PDB code: 7pqk was solved by A.Palencia, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.60 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.17, 61.8, 77.19, 90, 90, 90
R / Rfree (%) 13.7 / 16.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate (pdb code 7pqk). 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 Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate, PDB code: 7pqk:

Chlorine binding site 1 out of 1 in 7pqk

Go back to Chlorine Binding Sites List in 7pqk
Chlorine binding site 1 out of 1 in the Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Crystal Structure of M. Tuberculosis Leurs in Complex with the Adduct Formed By Prodrug CMPD1 with Adenosine-Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl601

b:14.9
occ:1.00
 CL A:81D601 0.0 14.9 1.0
C13 A:81D601 1.7 14.2 1.0
C14 A:81D601 2.7 14.4 1.0
C11 A:81D601 2.7 14.4 1.0
H141 A:81D601 2.8 17.3 1.0
HB A:VAL443 2.9 16.4 1.0
H332 A:81D601 2.9 17.8 1.0
HB2 A:HIS446 3.1 17.4 1.0
HB2 A:ARG338 3.1 17.2 1.0
HB2 A:ASP447 3.1 18.1 1.0
C10 A:81D601 3.2 14.2 1.0
HG21 A:THR341 3.3 16.7 1.0
HG3 A:ARG338 3.3 17.6 1.0
C33 A:81D601 3.5 14.9 1.0
HG11 A:VAL443 3.6 17.1 1.0
OG1 A:THR341 3.6 13.9 1.0
CB A:VAL443 3.7 13.6 1.0
CB A:ARG338 3.8 14.3 1.0
HB3 A:ARG338 3.8 17.2 1.0
HG21 A:VAL443 3.8 16.9 1.0
CB A:HIS446 3.8 14.5 1.0
HB3 A:HIS446 3.8 17.4 1.0
HG1 A:THR341 3.8 16.7 1.0
O A:HIS446 3.9 15.2 1.0
C A:HIS446 3.9 13.7 1.0
C15 A:81D601 4.0 16.0 1.0
CG A:ARG338 4.0 14.7 1.0
C12 A:81D601 4.0 14.5 1.0
CG1 A:VAL443 4.0 14.2 1.0
CB A:ASP447 4.1 15.0 1.0
CG2 A:THR341 4.1 13.9 1.0
HG12 A:VAL443 4.1 17.1 1.0
N A:ASP447 4.2 14.5 1.0
CG2 A:VAL443 4.2 14.1 1.0
H331 A:81D601 4.2 17.8 1.0
CB A:THR341 4.3 13.4 1.0
H341 A:81D601 4.3 17.4 1.0
HB3 A:ASP447 4.3 18.1 1.0
HB A:THR341 4.3 16.1 1.0
HG23 A:THR341 4.3 16.7 1.0
CA A:HIS446 4.4 14.2 1.0
HG2 A:ARG338 4.4 17.6 1.0
O A:VAL443 4.4 14.0 1.0
HG23 A:VAL443 4.4 16.9 1.0
N34 A:81D601 4.5 14.5 1.0
C16 A:81D601 4.5 15.0 1.0
H A:ASP447 4.6 17.4 1.0
O1 A:81D601 4.6 15.1 1.0
CA A:ASP447 4.6 15.0 1.0
HA A:ASP447 4.7 18.0 1.0
H A:HIS446 4.7 16.4 1.0
H151 A:81D601 4.7 19.2 1.0
HG22 A:THR341 4.8 16.7 1.0
HG13 A:VAL443 4.9 17.1 1.0
HH11 A:ARG338 4.9 20.5 1.0
CA A:VAL443 5.0 13.7 1.0
H A:VAL443 5.0 15.6 1.0

Reference:

G.Hoffmann, M.Le Gorrec, E.Mestdach, S.Cusack, L.Salmon, M.R.Jensen, A.Palencia. Adenosine-Dependent Activation Mechanism of Prodrugs Targeting An Aminoacyl-Trna Synthetase. J.Am.Chem.Soc. 2023.
ISSN: ESSN 1520-5126
PubMed: 36599057
DOI: 10.1021/JACS.2C04808
Page generated: Tue Jul 30 02:37:30 2024

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