Chlorine in PDB 5vjs: De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations

The structure of De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations, PDB code: 5vjs was solved by N.M.Ennist, P.L.Dutton, S.E.Stayrook, C.C.Moser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.43 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	43.749, 43.749, 245.737, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 27.8

The structure of De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Zinc	(Zn)	3 atoms

The binding sites of Chlorine atom in the De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations (pdb code 5vjs). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations, PDB code: 5vjs:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl205 b:42.6 occ:1.00 N A:ARG49 3.1 32.1 1.0 N A:ASN50 3.2 29.9 1.0 CB A:ASN50 3.7 35.7 1.0 CA A:ALA48 3.7 34.1 1.0 C A:ALA48 3.9 35.9 1.0 CA A:ARG49 4.0 35.7 1.0 CA A:ASN50 4.1 33.2 1.0 C A:ARG49 4.1 36.5 1.0 CD A:LYS53 4.1 41.2 1.0 CB A:ALA48 4.1 32.2 1.0 CB A:ARG49 4.5 41.2 1.0 CB A:LYS53 4.6 32.5 1.0 CG A:LYS53 4.7 39.5 1.0 O A:ASN50 4.7 32.1 1.0 O A:LYS47 4.9 34.3 1.0 C A:ASN50 4.9 32.6 1.0 N A:ALA48 5.0 32.1 1.0

Chlorine binding site 2 out of 3 in the De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl206 b:35.9 occ:1.00 NE A:ARG169 3.3 31.5 1.0 NH2 A:ARG169 3.6 30.6 1.0 CD2 A:LEU132 3.7 31.5 1.0 CZ A:ARG169 3.9 31.8 1.0 CG A:ARG169 4.1 30.2 1.0 CD A:ARG169 4.2 31.1 1.0 OE1 A:GLU136 4.7 43.5 1.0 OE2 A:GLU136 4.7 52.4 1.0 O A:HOH329 4.8 31.4 1.0 CG A:LEU132 4.8 25.4 1.0

Chlorine binding site 3 out of 3 in the De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of De Novo Photosynthetic Reaction Center Protein Equipped with Heme B, A Synthetic Zn Porphyrin, and Zn(II) Cations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl207 b:34.9 occ:1.00 ZN A:ZN203 2.4 30.5 1.0 OD2 A:ASP63 3.5 34.2 1.0 CD2 A:HIS138 3.5 24.3 1.0 NE2 A:HIS138 3.5 21.0 1.0 OD1 A:ASP134 3.5 34.4 1.0 CE A:LYS137 3.6 48.3 1.0 CE A:LYS59 3.6 37.5 1.0 CD1 A:LEU141 4.0 28.9 1.0 CB A:LYS137 4.0 32.2 1.0 NZ A:LYS137 4.2 56.7 1.0 CD A:LYS137 4.2 42.6 1.0 CG A:LYS59 4.4 33.1 1.0 CD A:LYS59 4.5 38.5 1.0 CG A:ASP63 4.6 30.2 1.0 NZ A:LYS59 4.6 40.1 1.0 CG A:ASP134 4.6 35.9 1.0 CG A:LYS137 4.7 38.0 1.0 CE1 A:HIS138 4.8 25.9 1.0 CG A:HIS138 4.8 24.8 1.0 CG A:LEU141 4.9 25.1 1.0 C A:LYS137 4.9 29.7 1.0 O A:ASP134 4.9 25.1 1.0 N A:HIS138 5.0 25.4 1.0

N.M.Ennist, Z.Zhao, S.E.Stayrook, P.L.Dutton, C.C.Moser. Design, Structure, and Action of An Artificial Photosynthetic Reaction Center Protein To Be Published.