Chlorine in PDB 3t1a: Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05

All present enzymatic activity of Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05:
2.7.7.49; 2.7.7.7; 3.1.26.13;

The structure of Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05, PDB code: 3t1a was solved by Y.Yan, J.Reid, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.14 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	118.330, 154.230, 155.680, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 25

The binding sites of Chlorine atom in the Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05 (pdb code 3t1a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05, PDB code: 3t1a:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05


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 Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl561 b:42.7 occ:1.00 CL1 A:5MA561 0.0 42.7 1.0 C A:5MA561 1.7 37.8 1.0 C5 A:5MA561 2.6 36.5 1.0 C1 A:5MA561 2.7 35.8 1.0 O A:5MA561 2.8 37.3 1.0 O A:TYR188 3.4 41.4 1.0 CD2 A:TYR181 3.4 41.7 1.0 C A:TYR188 3.4 42.2 1.0 N A:GLY190 3.5 40.3 1.0 C A:VAL189 3.7 43.7 1.0 N A:VAL189 3.7 41.0 1.0 CE2 A:TYR181 3.9 43.3 1.0 CA A:VAL189 3.9 41.0 1.0 C2 A:5MA561 4.0 32.9 1.0 CB A:TYR188 4.0 37.7 1.0 C4 A:5MA561 4.0 31.6 1.0 C7 A:5MA561 4.0 37.3 1.0 CA A:GLY190 4.0 41.0 1.0 O A:VAL179 4.1 46.2 1.0 O A:VAL189 4.2 42.9 1.0 CA A:TYR188 4.3 37.8 1.0 CB A:VAL179 4.4 47.0 1.0 C6 A:5MA561 4.4 36.6 1.0 CG1 A:VAL179 4.4 45.8 1.0 C3 A:5MA561 4.5 30.7 1.0 CB A:VAL106 4.5 46.0 1.0 CG A:TYR181 4.5 40.4 1.0 C A:VAL179 4.6 46.3 1.0 N A:TYR181 4.7 34.1 1.0 CB A:TYR181 4.8 37.3 1.0 CG2 A:VAL106 4.9 45.1 1.0 CG1 A:VAL106 4.9 44.8 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl561 b:41.9 occ:1.00 CL2 A:5MA561 0.0 41.9 1.0 C11 A:5MA561 1.7 39.6 1.0 C6 A:5MA561 2.6 36.6 1.0 C10 A:5MA561 2.7 41.3 1.0 CB A:PRO95 3.5 36.7 1.0 CD2 A:LEU100 3.8 36.8 1.0 CH2 A:TRP229 3.8 43.7 1.0 C7 A:5MA561 3.9 37.3 1.0 CG A:PRO95 3.9 40.3 1.0 C9 A:5MA561 3.9 43.4 1.0 CZ3 A:TRP229 4.1 43.4 1.0 CD1 A:TYR181 4.1 42.3 1.0 CZ2 A:TRP229 4.3 44.0 1.0 CG A:TYR181 4.3 40.4 1.0 C8 A:5MA561 4.4 42.1 1.0 CD1 A:LEU100 4.4 39.0 1.0 CD1 A:TYR188 4.4 40.1 1.0 CE1 A:TYR181 4.4 43.2 1.0 CG A:LEU100 4.6 38.6 1.0 CB A:TYR181 4.7 37.3 1.0 CE1 A:TYR188 4.7 39.5 1.0 CE3 A:TRP229 4.7 42.6 1.0 CD2 A:TYR181 4.8 41.7 1.0 CA A:PRO95 4.8 35.1 1.0 CD A:PRO95 4.8 36.0 1.0 CE2 A:TRP229 4.9 44.9 1.0 CZ A:TYR181 4.9 51.3 1.0 O A:PRO95 5.0 31.9 1.0 C A:PRO95 5.0 34.1 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Hiv-1 Reverse Transcriptase (K103N Mutant) in Complex with Inhibitor M05 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl561 b:43.4 occ:1.00 CL3 A:5MA561 0.0 43.4 1.0 C8 A:5MA561 1.7 42.1 1.0 C7 A:5MA561 2.7 37.3 1.0 C9 A:5MA561 2.7 43.4 1.0 O A:5MA561 2.9 37.3 1.0 C24 A:5MA561 3.0 44.3 1.0 N26 A:5MA561 3.1 44.4 1.0 CD2 A:PHE227 3.6 47.7 1.0 CG2 A:VAL108 3.6 43.6 1.0 N13 A:5MA561 3.7 31.8 1.0 C5 A:5MA561 3.8 36.5 1.0 CG2 A:VAL106 3.8 45.1 1.0 CE2 A:PHE227 3.9 49.9 1.0 C6 A:5MA561 3.9 36.6 1.0 C10 A:5MA561 4.0 41.3 1.0 CG A:PHE227 4.0 47.1 1.0 CB A:TYR188 4.0 37.7 1.0 C4 A:5MA561 4.1 31.6 1.0 CG A:TYR188 4.1 38.3 1.0 CD2 A:TYR188 4.2 39.7 1.0 C11 A:5MA561 4.4 39.6 1.0 CB A:PHE227 4.5 47.2 1.0 CZ A:PHE227 4.5 47.8 1.0 CD1 A:PHE227 4.6 49.5 1.0 CD1 A:LEU234 4.7 47.2 1.0 CD1 A:TYR188 4.8 40.1 1.0 CE1 A:PHE227 4.9 49.5 1.0 N12 A:5MA561 4.9 36.0 1.0 CE2 A:TYR188 4.9 40.6 1.0 C A:5MA561 5.0 37.8 1.0 CA A:TYR188 5.0 37.8 1.0

R.Gomez, S.J.Jolly, T.Williams, J.P.Vacca, M.Torrent, G.Mcgaughey, M.T.Lai, P.Felock, V.Munshi, D.Distefano, J.Flynn, M.Miller, Y.Yan, J.Reid, R.Sanchez, Y.Liang, B.Paton, B.L.Wan, N.Anthony. Design and Synthesis of Conformationally Constrained Inhibitors of Non-Nucleoside Reverse Transcriptase. J.Med.Chem. V. 54 7920 2011.
ISSN: ISSN 0022-2623
PubMed: 21985673
DOI: 10.1021/JM2010173