Chlorine in PDB 2y6x: Structure of PSB27 From Thermosynechococcus Elongatus

The structure of Structure of PSB27 From Thermosynechococcus Elongatus, PDB code: 2y6x was solved by F.Michoux, K.Takasaka, M.Boehm, P.J.Nixon, J.W.Murray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.31 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.930, 50.820, 53.070, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.8

The binding sites of Chlorine atom in the Structure of PSB27 From Thermosynechococcus Elongatus (pdb code 2y6x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of PSB27 From Thermosynechococcus Elongatus, PDB code: 2y6x:

Chlorine binding site 1 out of 1 in the Structure of PSB27 From Thermosynechococcus Elongatus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of PSB27 From Thermosynechococcus Elongatus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1135 b:22.7 occ:1.00 O A:HOH2048 3.1 29.4 1.0 N A:ASN106 3.2 22.2 1.0 O A:HOH2093 3.2 33.7 1.0 C A:TYR104 3.6 17.5 1.0 CA A:TYR104 3.6 17.9 1.0 N A:PRO105 3.6 18.7 1.0 CB A:ASN106 3.8 25.7 1.0 CA A:ASN106 3.8 24.0 1.0 CD A:PRO105 3.8 19.7 1.0 O A:HOH2091 3.8 40.1 1.0 N A:ARG107 3.9 19.4 1.0 CG A:ARG107 3.9 21.5 1.0 C A:ASN106 4.0 21.5 1.0 O A:TYR104 4.1 19.3 1.0 CB A:TYR104 4.2 18.0 1.0 C A:PRO105 4.3 22.9 1.0 CG A:PRO105 4.3 22.9 1.0 CD A:ARG107 4.4 21.7 1.0 CA A:PRO105 4.4 21.0 1.0 CD1 A:TYR104 4.5 21.7 1.0 ND2 A:ASN106 4.5 33.8 1.0 CB A:ARG107 4.6 18.1 1.0 CG A:ASN106 4.6 28.4 1.0 O A:ASN106 4.8 24.1 1.0 O A:SER103 4.8 20.0 1.0 N A:TYR104 4.9 18.8 1.0 CG A:TYR104 4.9 20.0 1.0 CA A:ARG107 4.9 19.0 1.0

F.Michoux, K.Takasaka, M.Boehm, J.Komenda, P.J.Nixon, J.W.Murray. Crystal Structure of the PSB27 Assembly Factor at 1.6A: Implications For Binding to Photosystem II. Photosynth.Res. V. 110 169 2012.
ISSN: ISSN 0166-8595
PubMed: 22193820
DOI: 10.1007/S11120-011-9712-7