Chlorine in PDB 4c00: Crystal Structure of Tama From E. Coli

The structure of Crystal Structure of Tama From E. Coli, PDB code: 4c00 was solved by F.Gruss, F.Zaehringer, R.P.Jakob, B.M.Burmann, S.Hiller, T.Maier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.269 / 2.25
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.470, 261.060, 57.840, 90.00, 90.00, 90.00
R / Rfree (%)	18.98 / 21.7

The binding sites of Chlorine atom in the Crystal Structure of Tama From E. Coli (pdb code 4c00). 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 Tama From E. Coli, PDB code: 4c00:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Tama From E. Coli


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 Tama From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:93.3 occ:1.00 HH12 A:ARG467 2.0 38.8 1.0 HH22 A:ARG467 2.3 49.8 1.0 OH A:TYR488 2.3 56.1 1.0 HA A:ASP460 2.6 56.4 1.0 HH A:TYR488 2.6 67.3 1.0 NH1 A:ARG467 2.8 32.3 1.0 NH2 A:ARG467 3.0 41.5 1.0 OD1 A:ASP460 3.0 58.3 1.0 HG13 A:ILE379 3.1 72.6 1.0 HG22 A:ILE379 3.2 76.9 1.0 CZ A:ARG467 3.3 37.8 1.0 HB A:ILE379 3.4 79.8 1.0 HH11 A:ARG467 3.5 38.8 1.0 CZ A:TYR488 3.5 51.2 1.0 HG3 A:LYS494 3.5 63.1 1.0 CA A:ASP460 3.5 47.0 1.0 HE1 A:TYR488 3.6 58.0 1.0 HE3 A:LYS494 3.6 78.8 1.0 HB3 A:GLN376 3.7 47.4 1.0 HH21 A:ARG467 3.7 49.8 1.0 HB3 A:ASP460 3.8 65.8 1.0 CG A:ASP460 3.8 66.5 1.0 O A:ASP460 3.9 50.3 1.0 CG1 A:ILE379 3.9 60.5 1.0 CB A:ASP460 3.9 54.8 1.0 CB A:ILE379 3.9 66.5 1.0 CG2 A:ILE379 4.0 64.1 1.0 CE1 A:TYR488 4.0 48.3 1.0 HG2 A:GLN376 4.1 49.3 1.0 C A:ASP460 4.2 50.4 1.0 HG12 A:ILE379 4.3 72.6 1.0 HG23 A:ILE379 4.4 76.9 1.0 CG A:LYS494 4.5 52.6 1.0 CE A:LYS494 4.5 65.7 1.0 HD2 A:PHE459 4.5 41.9 1.0 HE2 A:LYS494 4.5 78.8 1.0 HE1 A:PHE374 4.5 51.1 1.0 CB A:GLN376 4.5 39.5 1.0 N A:ASP460 4.5 38.9 1.0 NE A:ARG467 4.6 39.5 1.0 HG3 A:GLN376 4.6 49.3 1.0 CG A:GLN376 4.6 41.1 1.0 CE2 A:TYR488 4.6 50.1 1.0 O A:PHE459 4.7 37.5 1.0 HG21 A:ILE379 4.7 76.9 1.0 HG2 A:LYS494 4.7 63.1 1.0 O A:GLN376 4.7 47.0 1.0 HE2 A:TYR488 4.8 60.2 1.0 O A:LYS494 4.8 43.5 1.0 HA A:LYS494 4.9 49.2 1.0 HB2 A:ASP460 4.9 65.8 1.0 HB2 A:GLN376 4.9 47.4 1.0 O A:HOH2172 5.0 67.4 1.0 OD2 A:ASP460 5.0 80.6 1.0 C A:PHE459 5.0 41.6 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Tama From E. Coli


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 Tama From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:51.8 occ:1.00 H A:LEU320 2.4 41.2 1.0 H82 A:MC3615 2.6 0.8 1.0 H121 A:MC3613 2.8 0.5 1.0 HA A:LEU319 2.8 42.7 1.0 O A:HOH2040 3.0 47.7 1.0 H62 A:MC3615 3.1 78.0 1.0 O A:HOH2095 3.2 57.9 1.0 N A:LEU320 3.2 34.4 1.0 C8 A:MC3615 3.6 0.2 1.0 HB3 A:LEU320 3.6 40.9 1.0 HG A:LEU319 3.6 52.6 1.0 H81 A:MC3615 3.6 0.8 1.0 HB2 A:LEU320 3.7 40.9 1.0 CA A:LEU319 3.7 35.6 1.0 H63 A:MC3615 3.7 78.0 1.0 H72 A:MC3615 3.8 0.1 1.0 C6 A:MC3615 3.8 65.0 1.0 C12 A:MC3613 3.9 85.4 1.0 C A:LEU319 4.0 35.5 1.0 CB A:LEU320 4.0 34.0 1.0 H122 A:MC3613 4.0 0.5 1.0 HB3 A:LEU319 4.2 48.2 1.0 N A:MC3615 4.2 88.3 1.0 CA A:LEU320 4.2 33.6 1.0 CB A:LEU319 4.3 40.1 1.0 O A:PRO318 4.3 31.8 1.0 H83 A:MC3615 4.4 0.8 1.0 CG A:LEU319 4.4 43.9 1.0 H141 A:MC3613 4.4 0.7 1.0 C7 A:MC3615 4.5 87.6 1.0 C11 A:MC3613 4.6 76.4 1.0 H A:LYS321 4.7 51.5 1.0 H132 A:MC3613 4.7 0.4 1.0 HA A:LEU320 4.8 40.3 1.0 H61 A:MC3615 4.8 78.0 1.0 N A:LEU319 4.8 30.5 1.0 C13 A:MC3613 4.8 95.4 1.0 HD13 A:LEU319 4.8 53.7 1.0 C A:PRO318 5.0 30.3 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Tama From E. Coli


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 Tama From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:86.4 occ:1.00 HE A:ARG368 2.0 85.2 1.0 NE A:ARG368 2.8 71.0 1.0 HH21 A:ARG368 2.9 77.8 1.0 HB2 A:ARG368 3.1 53.4 1.0 O A:HOH2128 3.1 73.2 1.0 O A:HOH2138 3.1 48.2 1.0 HB3 A:ASN366 3.5 40.7 1.0 NH2 A:ARG368 3.5 65.0 1.0 HD2 A:ARG368 3.6 96.2 1.0 CZ A:ARG368 3.6 64.3 1.0 CD A:ARG368 3.8 80.2 1.0 OD1 A:ASP414 3.8 45.7 1.0 HB2 A:ASN366 3.8 40.7 1.0 CB A:ARG368 3.9 44.5 1.0 HB3 A:ARG368 3.9 53.4 1.0 HE2 A:TYR387 4.1 35.5 1.0 CB A:ASN366 4.1 33.9 1.0 HG12 A:VAL350 4.1 48.7 1.0 O A:HOH2125 4.1 33.7 1.0 HG11 A:VAL350 4.1 48.7 1.0 HD21 A:ASN366 4.2 44.0 1.0 HH22 A:ARG368 4.3 77.8 1.0 CG A:ARG368 4.4 63.8 1.0 O A:HOH2127 4.4 75.4 1.0 HH A:TYR387 4.4 52.2 1.0 ND2 A:ASN366 4.4 36.6 1.0 O A:HOH2146 4.4 65.2 1.0 CG A:ASN366 4.4 40.8 1.0 HD3 A:ARG368 4.6 96.2 1.0 CG1 A:VAL350 4.6 40.5 1.0 CG A:ASP414 4.6 51.0 1.0 CE2 A:TYR387 4.6 29.6 1.0 HG3 A:ARG368 4.7 76.5 1.0 O A:HOH2139 4.8 72.8 1.0 O A:HOH2126 4.8 61.5 1.0 OD2 A:ASP414 4.9 58.7 1.0 HG22 A:VAL350 4.9 67.3 1.0 NH1 A:ARG368 4.9 64.8 1.0 OH A:TYR387 4.9 43.5 1.0 HG23 A:VAL350 5.0 67.3 1.0 HD22 A:ASN366 5.0 44.0 1.0

F.Gruss, F.Zaehringer, R.P.Jakob, B.M.Burmann, S.Hiller, T.Maier. The Structural Basis of Autotransporter Translocation By Tama Nat.Struct.Mol.Biol. V. 20 1318 2013.
ISSN: ISSN 1545-9993
PubMed: 24056943
DOI: 10.1038/NSMB.2689