Chlorine in PDB 3iix: X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine

The structure of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine, PDB code: 3iix 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)	58.22 / 1.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.054, 78.925, 86.192, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.6

The structure of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Chlorine atom in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine (pdb code 3iix). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine, PDB code: 3iix:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine


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 Methionine and 5'Deoxyadenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl349 b:30.6 occ:1.00 O A:HOH570 2.3 25.7 1.0 O A:HOH585 2.8 23.7 1.0 O A:HOH677 3.1 38.6 1.0 N A:ALA270 3.2 12.9 1.0 OH A:TYR306 3.4 19.4 1.0 CB A:ALA270 3.5 12.4 1.0 CB A:THR268 3.7 12.0 1.0 N A:THR269 3.7 13.5 1.0 NH2 A:ARG159 3.9 18.2 1.0 O A:HOH499 3.9 18.5 1.0 CA A:ALA270 4.0 12.4 1.0 CE2 A:TYR306 4.0 15.8 1.0 OG1 A:THR268 4.1 12.8 1.0 CZ A:TYR306 4.2 16.9 1.0 C A:THR269 4.2 14.7 1.0 CA A:THR269 4.3 15.1 1.0 C A:THR268 4.3 12.1 1.0 CB A:THR269 4.3 16.0 1.0 O A:HOH558 4.4 22.4 1.0 O A:HOH595 4.5 23.1 1.0 CG2 A:THR268 4.5 13.1 1.0 CA A:THR268 4.5 11.9 1.0 O A:HOH615 4.6 28.6 1.0 CZ A:ARG159 4.8 16.0 1.0 NH1 A:ARG159 4.9 15.8 1.0 O4' A:5AD1501 5.0 10.2 1.0 O A:HOH697 5.0 31.6 1.0

Chlorine binding site 2 out of 4 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine


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 Methionine and 5'Deoxyadenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl350 b:13.8 occ:1.00 O A:HOH722 3.1 26.0 0.5 OG1 A:THR134 3.1 10.2 1.0 O A:HOH500 3.2 15.6 1.0 NH1 A:ARG155 3.4 9.5 1.0 NE A:ARG54 3.6 11.0 1.0 SD A:MET224 3.8 12.8 0.6 CD A:ARG54 3.8 11.7 1.0 CD A:ARG155 3.9 10.6 1.0 CG2 A:THR134 3.9 9.1 1.0 CB A:THR134 3.9 8.6 1.0 CG2 A:THR103 4.0 9.6 1.0 CG A:ARG54 4.0 10.9 1.0 CZ A:ARG54 4.1 10.7 1.0 O A:HOH622 4.2 30.7 1.0 CZ A:ARG155 4.4 9.1 1.0 CG2 A:VAL105 4.4 10.2 1.0 NH2 A:ARG54 4.5 12.2 1.0 NE A:ARG155 4.5 10.9 1.0 CB A:ARG54 4.5 10.5 1.0 CE A:MET224 4.5 12.8 0.4 CE A:MET291 4.6 15.4 0.3 CD2 A:LEU157 4.7 16.6 1.0 CG A:ARG155 4.8 11.0 1.0 CB A:ARG155 4.8 9.4 1.0 NH1 A:ARG54 4.8 11.2 1.0 CB A:THR103 5.0 9.3 1.0 CE A:MET224 5.0 12.4 0.6 CD1 A:LEU157 5.0 15.3 1.0

Chlorine binding site 3 out of 4 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine


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 Methionine and 5'Deoxyadenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl351 b:26.7 occ:0.65 CL A:CL351 0.0 26.7 0.7 CL A:CL351 0.8 30.4 0.3 O A:HOH542 2.9 18.6 1.0 O A:HOH712 3.1 36.9 1.0 O A:HOH552 3.3 17.4 1.0 O A:HOH750 3.4 32.5 1.0 NH2 A:ARG159 3.5 18.2 1.0 CE A:MET291 3.6 18.4 0.3 CG A:PRO266 3.7 8.2 0.5 SD A:MET291 3.7 16.8 0.3 O A:HOH677 3.8 38.6 1.0 CA A:GLY226 3.9 9.8 1.0 CE A:MET291 3.9 17.6 0.3 CG A:PRO266 4.0 10.2 0.5 NE A:ARG159 4.1 15.5 1.0 CG2 A:THR268 4.1 13.1 1.0 CE A:MET291 4.1 15.4 0.3 CZ A:ARG159 4.3 16.0 1.0 CB A:PRO266 4.4 8.8 0.5 CB A:PRO266 4.5 9.3 0.5 O A:HOH498 4.5 15.9 1.0 O A:HOH622 4.6 30.7 1.0 SD A:MET291 4.7 14.7 0.3 O A:HOH615 4.7 28.6 1.0 CD A:PRO266 4.8 9.7 0.5 CD A:PRO266 4.8 10.0 0.5 N A:GLY226 4.8 9.8 1.0 CD1 A:LEU157 4.8 15.3 1.0 C A:GLY226 4.8 10.4 1.0

Chlorine binding site 4 out of 4 in the X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of X-Ray Structure of the Fefe-Hydrogenase Maturase Hyde From T. Maritima in Complex with Methionine and 5'Deoxyadenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl351 b:30.4 occ:0.35 CL A:CL351 0.0 30.4 0.3 CL A:CL351 0.8 26.7 0.7 O A:HOH542 2.8 18.6 1.0 NH2 A:ARG159 2.8 18.2 1.0 O A:HOH750 2.9 32.5 1.0 O A:HOH712 3.2 36.9 1.0 O A:HOH677 3.4 38.6 1.0 NE A:ARG159 3.5 15.5 1.0 CZ A:ARG159 3.6 16.0 1.0 CG2 A:THR268 4.0 13.1 1.0 CE A:MET291 4.0 18.4 0.3 O A:HOH552 4.0 17.4 1.0 CE A:MET291 4.1 17.6 0.3 O A:HOH615 4.1 28.6 1.0 CA A:GLY226 4.1 9.8 1.0 SD A:MET291 4.2 16.8 0.3 CG A:PRO266 4.3 8.2 0.5 CE A:MET291 4.7 15.4 0.3 CG A:PRO266 4.8 10.2 0.5 O A:HOH508 4.8 16.0 1.0 C A:GLY226 4.8 10.4 1.0 CD A:ARG159 4.8 13.7 1.0 O A:HOH498 4.9 15.9 1.0 NH1 A:ARG159 4.9 15.8 1.0 CB A:THR268 5.0 12.0 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