Chlorine in PDB 6ero: Structure of Human TFB2M

The structure of Structure of Human TFB2M, PDB code: 6ero was solved by H.S.Hillen, Y.I.Morozov, A.Sarfallah, D.Temiakov, P.Cramer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.53 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.950, 165.650, 44.730, 90.00, 97.97, 90.00
R / Rfree (%)	19.2 / 21.4

The binding sites of Chlorine atom in the Structure of Human TFB2M (pdb code 6ero). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Human TFB2M, PDB code: 6ero:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Human TFB2M


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human TFB2M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:51.4 occ:1.00 H A:ALA264 2.3 44.9 1.0 HA A:ASP263 3.0 44.4 1.0 N A:ALA264 3.2 37.1 1.0 HE A:ARG257 3.3 77.5 1.0 HB3 A:ALA264 3.3 48.6 1.0 HG2 A:ARG257 3.6 64.1 1.0 HB2 A:ALA264 3.7 48.6 1.0 CB A:ALA264 3.8 40.2 1.0 CA A:ASP263 3.9 36.8 1.0 C A:ASP263 4.0 37.5 1.0 H A:ARG265 4.0 46.3 1.0 NE A:ARG257 4.1 64.3 1.0 HH21 A:ARG257 4.1 83.4 1.0 CA A:ALA264 4.1 37.9 1.0 O A:LEU262 4.1 37.0 1.0 CG A:ARG257 4.3 53.1 1.0 HG3 A:ARG257 4.4 64.1 1.0 OD1 A:ASP263 4.4 44.5 1.0 CG A:ASP263 4.6 43.1 1.0 N A:ARG265 4.7 38.3 1.0 NH2 A:ARG257 4.8 69.2 1.0 HB1 A:ALA264 4.8 48.6 1.0 CD A:ARG257 4.8 60.5 1.0 CB A:ASP263 4.8 40.9 1.0 HA A:ALA264 4.8 45.9 1.0 N A:ASP263 4.8 35.9 1.0 C A:LEU262 4.9 36.0 1.0 CZ A:ARG257 4.9 67.8 1.0 HD11 A:ILE253 4.9 58.3 1.0 C A:ALA264 5.0 35.0 1.0

Chlorine binding site 2 out of 2 in the Structure of Human TFB2M


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Human TFB2M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:53.2 occ:1.00 H A:LYS303 2.5 49.8 1.0 H A:TRP304 2.6 48.9 1.0 HB2 A:TYR302 3.0 50.2 1.0 N A:LYS303 3.3 43.1 1.0 HA A:TYR302 3.3 51.6 1.0 N A:TRP304 3.4 42.4 1.0 HD1 A:TRP304 3.4 50.0 1.0 HB2 A:TRP304 3.4 49.2 1.0 H11 A:GOL403 3.5 88.7 1.0 HO2 A:GOL403 3.7 86.2 1.0 CB A:TYR302 3.8 43.5 1.0 CA A:TYR302 3.8 43.7 1.0 HB2 A:LYS303 3.9 51.9 1.0 O A:TRP304 3.9 42.4 1.0 O A:HOH519 4.0 47.3 1.0 C A:TYR302 4.0 43.1 1.0 HB3 A:TYR302 4.1 50.2 1.0 CB A:TRP304 4.2 42.7 1.0 CA A:LYS303 4.2 42.7 1.0 O2 A:GOL403 4.2 71.5 1.0 CD1 A:TRP304 4.2 43.4 1.0 CA A:TRP304 4.2 42.2 1.0 C A:LYS303 4.3 42.2 1.0 CB A:LYS303 4.5 43.2 1.0 C A:TRP304 4.5 42.1 1.0 C1 A:GOL403 4.6 73.5 1.0 CG A:TRP304 4.6 42.8 1.0 HG3 A:LYS303 4.6 59.4 1.0 HD2 A:TYR302 4.7 48.6 1.0 HD2 A:LYS303 4.9 66.7 1.0 HB3 A:TRP304 5.0 49.2 1.0

H.S.Hillen, Y.I.Morozov, A.Sarfallah, D.Temiakov, P.Cramer. Structural Basis of Mitochondrial Transcription Initiation. Cell V. 171 1072 2017.
ISSN: ISSN 1097-4172
PubMed: 29149603
DOI: 10.1016/J.CELL.2017.10.036