Chlorine in PDB 6wz1: Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3

The structure of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz1 was solved by F.A.Tezcan, A.Kakkis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.79 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.759, 77.392, 47.940, 90.00, 110.70, 90.00
R / Rfree (%)	17.6 / 22.9

The structure of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 also contains other interesting chemical elements:

Manganese	(Mn)	1 atom
Iron	(Fe)	3 atoms
Calcium	(Ca)	4 atoms

The binding sites of Chlorine atom in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 (pdb code 6wz1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3, PDB code: 6wz1:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:32.5 occ:1.00 NH1 A:ARG34 3.2 18.1 1.0 CA A:HIS73 3.5 17.3 1.0 CB A:ALA76 3.6 20.9 1.0 CB A:HIS73 3.7 19.5 1.0 CD2 A:HIS73 3.8 18.9 1.0 CD A:ARG34 3.9 18.4 1.0 CG A:HIS73 4.1 23.8 1.0 CZ A:ARG34 4.3 16.9 1.0 N A:HIS73 4.3 13.6 1.0 O A:HIS73 4.5 14.6 1.0 NE A:ARG34 4.5 18.6 1.0 CZ3 C:TRP70 4.5 15.9 1.0 C A:HIS73 4.5 21.4 1.0 O A:HOH320 4.6 27.4 1.0 OD1 C:ASP74 4.7 18.7 1.0 O A:ILE72 4.8 15.3 1.0 C A:ILE72 4.8 15.1 1.0 CE3 C:TRP70 4.9 14.8 1.0 CG A:ARG34 4.9 20.5 1.0 CE1 C:HIS73 4.9 32.5 1.0 CG2 A:ILE72 5.0 15.7 1.0

Chlorine binding site 2 out of 4 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl204 b:20.6 occ:1.00 NH2 B:ARG62 3.3 12.1 1.0 O C:HOH361 3.3 21.7 1.0 NH2 C:ARG62 3.3 15.6 1.0 O A:HOH331 3.4 21.4 1.0 O B:HOH362 3.5 21.1 1.0 NH2 A:ARG62 3.5 13.9 1.0 NE A:ARG62 3.9 14.2 1.0 NE B:ARG62 4.0 13.8 1.0 NE C:ARG62 4.0 13.5 1.0 CZ B:ARG62 4.0 18.0 1.0 CD1 C:ILE59 4.0 12.7 1.0 CZ C:ARG62 4.0 11.9 1.0 CZ A:ARG62 4.1 14.1 1.0 CD1 B:ILE59 4.3 19.3 1.0 CD1 A:ILE59 4.5 23.8 1.0 CB C:ALA54 4.7 15.3 1.0 CG1 A:ILE59 4.8 25.1 1.0 CG1 B:ILE59 4.9 22.4 1.0

Chlorine binding site 3 out of 4 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl205 b:22.4 occ:1.00 NZ C:LYS41 3.1 17.2 1.0 NZ A:LYS41 3.2 14.3 1.0 O B:HOH362 3.3 21.1 1.0 NZ B:LYS41 3.3 16.9 1.0 O C:HOH361 3.5 21.7 1.0 CE C:LYS41 3.6 10.3 1.0 CE A:LYS41 3.8 13.4 1.0 O A:HOH331 3.9 21.4 1.0 CE B:LYS41 4.2 13.5 1.0 OD2 B:ASP66 4.2 17.1 1.0 OD2 C:ASP66 4.4 14.3 1.0 OD2 A:ASP66 4.4 13.7 1.0

Chlorine binding site 4 out of 4 in the Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Mn-Bound Structure of An Engineered Protein Trimer, TRICYT3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl202 b:52.4 occ:1.00 O C:HOH351 2.9 16.5 1.0 NE C:ARG106 3.0 9.4 1.0 O C:HOH332 3.5 23.0 1.0 CG C:ARG106 3.6 12.8 1.0 CD C:ARG106 3.8 17.7 1.0 CZ C:ARG106 3.9 11.2 1.0 NH2 C:ARG106 3.9 9.4 1.0 CB C:ARG106 4.1 14.8 1.0 O C:ARG106 4.5 22.4 1.0 C C:ARG106 4.6 22.5 1.0 OXT C:ARG106 4.9 21.2 1.0

F.A.Tezcan, A.Kakkis, D.Gagnon, J.Esselborn, R.D.Britt. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32830423
DOI: 10.1002/ANIE.202009226