Chlorine in PDB 3iiz: X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine

The structure of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine, PDB code: 3iiz was solved by Y.Nicolet, P.Amara, J.M.Mouesca, J.C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.16 / 1.62
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.628, 78.780, 85.943, 90.00, 90.00, 90.00
R / Rfree (%)	13.8 / 18.4

The structure of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine also contains other interesting chemical elements:

Iron

(Fe)

6 atoms

The binding sites of Chlorine atom in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine (pdb code 3iiz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine, PDB code: 3iiz:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl349 b:11.9 occ:1.00 OG1 A:THR134 3.0 9.7 1.0 O A:HOH485 3.2 12.5 1.0 NH1 A:ARG155 3.2 10.2 1.0 NE A:ARG54 3.4 11.2 1.0 CD A:ARG54 3.7 9.9 1.0 CD A:ARG155 3.8 10.6 1.0 SD A:MET224 3.8 7.4 0.2 CB A:THR134 3.8 10.2 1.0 CG2 A:THR103 3.9 8.8 1.0 CG2 A:THR134 3.9 9.6 1.0 CZ A:ARG54 3.9 10.7 1.0 CG A:ARG54 3.9 10.2 1.0 CZ A:ARG155 4.2 10.9 1.0 NH2 A:ARG54 4.3 9.9 1.0 O A:HOH708 4.4 35.2 1.0 NE A:ARG155 4.4 10.8 1.0 CB A:ARG54 4.4 10.3 1.0 CG2 A:VAL105 4.5 8.7 1.0 CE A:MET224 4.6 19.1 0.8 CG A:ARG155 4.7 9.3 1.0 NH1 A:ARG54 4.7 10.0 1.0 CD2 A:LEU157 4.8 17.4 1.0 CB A:ARG155 4.8 8.8 1.0 CB A:THR103 4.8 8.9 1.0 OG1 A:THR103 4.9 8.8 1.0 CE A:MET224 5.0 6.8 0.2

Chlorine binding site 2 out of 3 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl350 b:27.4 occ:0.70 CL A:CL350 0.0 27.4 0.7 CL A:CL350 1.6 32.7 0.3 O A:HOH435 2.4 53.4 1.0 N A:ALA270 3.3 12.7 1.0 OH A:TYR306 3.5 19.9 1.0 CB A:ALA270 3.6 11.2 1.0 NH2 A:ARG159 3.6 14.2 0.5 O A:HOH475 3.7 23.8 1.0 O A:HOH780 3.7 35.6 1.0 NH2 A:ARG159 3.7 19.8 0.5 N A:THR269 3.7 13.0 1.0 CB A:THR268 3.7 10.9 1.0 CA A:ALA270 4.0 11.9 1.0 NH1 A:ARG159 4.1 14.2 0.5 O A:HOH781 4.1 48.2 1.0 CB A:THR269 4.2 16.2 1.0 OG1 A:THR268 4.2 11.5 1.0 C A:THR269 4.2 13.2 1.0 CA A:THR269 4.2 14.4 1.0 CE2 A:TYR306 4.2 16.3 1.0 CZ A:TYR306 4.3 17.7 1.0 C A:THR268 4.3 11.3 1.0 CZ A:ARG159 4.3 14.4 0.5 O A:HOH710 4.4 36.0 1.0 CA A:THR268 4.5 10.7 1.0 CG2 A:THR268 4.5 10.9 1.0 O A:HOH673 4.6 42.5 1.0 CZ A:ARG159 4.7 19.7 0.5 O A:HOH709 4.9 35.2 1.0 OG1 A:THR269 4.9 18.7 1.0

Chlorine binding site 3 out of 3 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with S-Adenosyl-L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl350 b:32.7 occ:0.30 CL A:CL350 0.0 32.7 0.3 CL A:CL350 1.6 27.4 0.7 O A:HOH435 2.6 53.4 1.0 O A:HOH710 3.1 36.0 1.0 O A:HOH709 3.4 35.2 1.0 N A:THR269 3.4 13.0 1.0 O A:HOH780 3.5 35.6 1.0 CB A:THR269 3.7 16.2 1.0 NH2 A:ARG159 3.7 14.2 0.5 O A:HOH781 3.7 48.2 1.0 CB A:THR268 3.9 10.9 1.0 O A:HOH673 4.0 42.5 1.0 OG1 A:THR269 4.0 18.7 1.0 CA A:THR269 4.0 14.4 1.0 OH A:TYR306 4.1 19.9 1.0 N A:ALA270 4.1 12.7 1.0 NH2 A:ARG159 4.2 19.8 0.5 C A:THR268 4.3 11.3 1.0 CA A:THR268 4.3 10.7 1.0 O A:HOH742 4.5 25.9 1.0 O A:HOH364 4.5 49.5 1.0 C A:THR269 4.6 13.2 1.0 CG2 A:THR268 4.6 10.9 1.0 CZ A:ARG159 4.7 14.4 0.5 NH1 A:ARG159 4.8 14.2 0.5 OG1 A:THR268 4.8 11.5 1.0 O A:HOH484 4.9 20.2 1.0 CG2 A:THR269 4.9 19.5 1.0

Y.Nicolet, P.Amara, J.-M.Mouesca, J.C.Fontecilla-Camps. Unexpected Electron Transfer Mechanism Upon Adomet Cleavage in Radical Sam Proteins Proc.Natl.Acad.Sci.Usa 2009.
ISSN: ESSN 1091-6490
PubMed: 19706452
DOI: 10.1073/PNAS.0904385106