Chlorine in PDB 8pne: E.Coli Yihx Wild Type Apo

All present enzymatic activity of E.Coli Yihx Wild Type Apo:
3.1.3.10;

The structure of E.Coli Yihx Wild Type Apo, PDB code: 8pne was solved by D.Zappala, P.Baumann, Y.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.20 / 1.90
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.216, 79.567, 148.188, 90, 90, 90
R / Rfree (%)	20.4 / 23.4

The structure of E.Coli Yihx Wild Type Apo also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the E.Coli Yihx Wild Type Apo (pdb code 8pne). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the E.Coli Yihx Wild Type Apo, PDB code: 8pne:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the E.Coli Yihx Wild Type Apo


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E.Coli Yihx Wild Type Apo within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl307 b:51.6 occ:1.00 O A:HOH514 2.8 37.3 1.0 CL A:CL308 2.9 61.8 1.0 NZ A:LYS141 3.1 40.7 1.0 N A:ASN108 3.1 30.7 1.0 OD1 A:ASP6 3.3 42.7 1.0 CE A:LYS141 3.3 38.6 1.0 O A:HOH451 3.4 34.7 1.0 O A:HOH535 3.4 47.0 1.0 CB A:ASN108 3.5 31.7 1.0 O A:ASN108 3.7 36.7 1.0 O A:HOH466 3.8 39.4 1.0 CA A:ASN108 3.8 31.8 1.0 CA A:SER107 3.9 33.5 1.0 CG A:ASN108 4.0 36.4 1.0 C A:SER107 4.0 32.1 1.0 C A:ASN108 4.2 36.4 1.0 OG A:SER107 4.3 35.1 1.0 ND2 A:ASN108 4.3 37.0 1.0 CG A:ASP6 4.3 38.0 1.0 O A:HOH452 4.3 39.6 1.0 O A:LEU106 4.5 30.3 1.0 OD1 A:ASN108 4.6 37.9 1.0 CB A:SER107 4.6 38.4 1.0 O A:HOH512 4.6 61.5 1.0 ND2 A:ASN170 4.8 51.7 1.0 OD2 A:ASP6 4.8 41.8 1.0 CD A:LYS141 4.8 38.2 1.0 C4 A:PEG301 4.9 59.3 1.0 MG A:MG305 4.9 42.5 1.0

Chlorine binding site 2 out of 4 in the E.Coli Yihx Wild Type Apo


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of E.Coli Yihx Wild Type Apo within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl308 b:61.8 occ:1.00 C4 A:PEG301 2.8 59.3 1.0 OG A:SER107 2.9 35.1 1.0 CL A:CL307 2.9 51.6 1.0 O4 A:PEG301 2.9 57.0 1.0 N A:GLY8 3.1 40.8 1.0 O A:HOH451 3.3 34.7 1.0 OD1 A:ASP6 3.4 42.7 1.0 CB A:LEU7 3.6 42.2 1.0 CB A:SER107 3.6 38.4 1.0 O A:HOH535 3.6 47.0 1.0 O A:ASN108 3.8 36.7 1.0 CA A:GLY8 3.8 45.2 1.0 N A:LEU7 4.0 40.6 1.0 CA A:SER107 4.0 33.5 1.0 C A:LEU7 4.1 37.5 1.0 CA A:LEU7 4.1 40.1 1.0 C3 A:PEG301 4.2 62.2 1.0 O A:HOH437 4.2 39.9 1.0 N A:ASN108 4.3 30.7 1.0 O A:HOH466 4.3 39.4 1.0 CG A:LEU7 4.4 47.5 1.0 CG A:ASP6 4.6 38.0 1.0 C A:SER107 4.6 32.1 1.0 C A:ASN108 4.7 36.4 1.0 CD2 A:LEU7 4.7 50.2 1.0 O2 A:PEG301 4.9 46.8 1.0 O A:HOH488 5.0 45.1 1.0 NZ A:LYS141 5.0 40.7 1.0 C A:GLY8 5.0 52.6 1.0

Chlorine binding site 3 out of 4 in the E.Coli Yihx Wild Type Apo


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of E.Coli Yihx Wild Type Apo within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl309 b:51.8 occ:1.00 O A:HOH523 3.0 45.7 1.0 N A:ARG145 3.4 31.8 1.0 CG A:ARG145 3.4 33.3 1.0 CB A:ARG145 3.6 33.8 1.0 O A:HOH478 3.6 48.8 1.0 N A:ALA144 3.7 41.3 1.0 CD A:ARG145 3.8 29.8 1.0 CA A:ARG145 4.1 34.5 1.0 CB A:GLU143 4.1 36.0 1.0 O A:HOH561 4.2 63.9 1.0 CB A:ALA144 4.3 40.4 1.0 NE A:ARG145 4.3 31.5 1.0 CA A:ALA144 4.3 36.1 1.0 C A:ALA144 4.3 31.7 1.0 C A:GLU143 4.3 41.1 1.0 CA A:GLU143 4.6 38.6 1.0 CG A:GLU143 4.9 36.9 1.0

Chlorine binding site 4 out of 4 in the E.Coli Yihx Wild Type Apo


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of E.Coli Yihx Wild Type Apo within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl310 b:83.2 occ:1.00 CD A:ARG28 3.4 58.7 1.0 NH1 A:ARG28 3.5 61.2 1.0 CB A:ARG28 4.1 40.0 1.0 CG A:ARG28 4.3 50.7 1.0 NE A:ARG28 4.3 65.9 1.0 CZ A:ARG28 4.4 67.3 1.0

D.Zappala, P.Baumann, Y.Jin. Apo Structure of E.Coli Yihx Wild Type To Be Published.