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Chlorine in PDB 2arl: The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding

Protein crystallography data

The structure of The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding, PDB code: 2arl was solved by P.G.Wilmann, J.Battad, T.Beddoe, S.Olsen, S.C.Smith, S.Dove, R.J.Devenish, J.Rossjohn, M.Prescott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 42 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.770, 92.770, 75.020, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 25.3

Other elements in 2arl:

The structure of The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding also contains other interesting chemical elements:

Iodine (I) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding (pdb code 2arl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding, PDB code: 2arl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2arl

Go back to Chlorine Binding Sites List in 2arl
Chlorine binding site 1 out of 2 in the The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl511

b:27.2
occ:1.00
N A:GLY155 3.4 32.5 1.0
O A:HOH650 3.6 51.9 1.0
CG A:MET189 3.8 39.9 1.0
N A:GLY154 3.9 31.6 1.0
CA A:GLY155 4.0 33.7 1.0
O A:HOH620 4.0 44.4 1.0
N A:ARG153 4.1 31.7 1.0
CB A:ALA152 4.1 32.2 1.0
CE A:MET189 4.1 40.5 1.0
C A:ARG153 4.2 30.5 1.0
CA A:ARG153 4.2 31.7 1.0
C A:ALA152 4.3 31.2 1.0
C A:GLY154 4.4 33.8 1.0
CA A:GLY154 4.5 32.3 1.0
CB A:MET189 4.5 40.6 1.0
O A:ALA152 4.6 31.4 1.0
SD A:MET189 4.7 41.0 1.0
CA A:ALA152 4.8 31.8 1.0
C A:GLY155 4.9 34.7 1.0
O A:ARG153 4.9 30.3 1.0
N A:MET156 5.0 34.6 1.0

Chlorine binding site 2 out of 2 in 2arl

Go back to Chlorine Binding Sites List in 2arl
Chlorine binding site 2 out of 2 in the The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl512

b:38.5
occ:1.00
N A:GLY191 3.5 37.4 1.0
CA A:GLY191 3.8 36.4 1.0
CG1 A:ILE79 3.9 44.0 1.0
O A:ASP78 4.0 48.1 1.0
CG2 A:ILE79 4.1 42.7 1.0
CA A:ILE79 4.2 44.9 1.0
CB A:ILE79 4.3 44.1 1.0
C A:GLY191 4.4 36.1 1.0
CD A:PRO80 4.4 44.0 1.0
CE A:LYS221 4.5 47.3 1.0
O A:GLY191 4.5 35.1 1.0
NZ A:LYS221 4.6 48.4 1.0
C A:PRO190 4.7 37.9 1.0
CD1 A:ILE79 4.8 44.7 1.0
C A:ASP78 4.9 48.2 1.0

Reference:

P.G.Wilmann, J.Battad, T.Beddoe, S.Olsen, S.C.Smith, S.Dove, R.J.Devenish, J.Rossjohn, M.Prescott. The 2.0 Angstroms Crystal Structure of A Pocilloporin at pH 3.5: the Structural Basis For the Linkage Between Color Transition and Halide Binding Photochem.Photobiol. V. 82 359 2006.
ISSN: ISSN 0031-8655
PubMed: 16613486
DOI: 10.1562/2005-05-02-RA-509
Page generated: Thu Jul 10 21:12:54 2025

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