Iron in PDB 1ds8: Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+

The structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+, PDB code: 1ds8 was solved by H.L.Axelrod, E.C.Abresch, M.L.Paddock, M.Y.Okamura, G.Feher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	139.590, 139.590, 272.860, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 25.6

The structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+ also contains other interesting chemical elements:

Cadmium	(Cd)	2 atoms
Magnesium	(Mg)	8 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Iron atom in the Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+ (pdb code 1ds8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+, PDB code: 1ds8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+ within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe1007 b:28.2 occ:1.00 NE2 M:HIS219 2.1 29.7 1.0 NE2 L:HIS190 2.1 29.8 1.0 NE2 M:HIS266 2.2 29.1 1.0 OE2 M:GLU234 2.2 31.4 1.0 NE2 L:HIS230 2.2 27.9 1.0 OE1 M:GLU234 2.3 30.9 1.0 CD M:GLU234 2.6 31.4 1.0 CE1 L:HIS190 3.0 30.2 1.0 CE1 M:HIS219 3.0 29.9 1.0 CE1 M:HIS266 3.0 29.5 1.0 CD2 M:HIS219 3.2 29.2 1.0 CE1 L:HIS230 3.2 27.5 1.0 CD2 L:HIS190 3.2 29.8 1.0 CD2 M:HIS266 3.3 29.7 1.0 CD2 L:HIS230 3.3 27.6 1.0 CG M:GLU234 4.1 31.6 1.0 ND1 M:HIS219 4.2 30.0 1.0 ND1 L:HIS190 4.2 31.0 1.0 ND1 M:HIS266 4.2 29.8 1.0 CG M:HIS219 4.2 30.0 1.0 CG L:HIS190 4.3 29.9 1.0 ND1 L:HIS230 4.3 27.1 1.0 CG M:HIS266 4.3 30.2 1.0 CG1 M:ILE223 4.4 29.8 1.0 CG L:HIS230 4.4 28.0 1.0 CG2 L:VAL194 4.6 28.8 1.0 O M:HOH1049 4.7 25.5 1.0 CD1 M:ILE223 4.8 29.8 1.0 CB M:GLU234 4.9 32.2 1.0

Iron binding site 2 out of 2 in the Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor CD2+ within 5.0Å range: probe atom residue distance (Å) B Occ S:Fe2007 b:32.7 occ:1.00 NE2 R:HIS190 2.0 32.3 1.0 NE2 S:HIS219 2.1 30.7 1.0 NE2 S:HIS266 2.2 31.7 1.0 OE2 S:GLU234 2.2 34.2 1.0 NE2 R:HIS230 2.2 30.9 1.0 OE1 S:GLU234 2.3 33.9 1.0 CD S:GLU234 2.5 33.7 1.0 CE1 R:HIS190 2.9 32.3 1.0 CE1 S:HIS266 3.0 31.6 1.0 CE1 S:HIS219 3.0 30.3 1.0 CD2 R:HIS190 3.1 31.9 1.0 CE1 R:HIS230 3.2 30.9 1.0 CD2 S:HIS219 3.2 30.6 1.0 CD2 S:HIS266 3.3 31.4 1.0 CD2 R:HIS230 3.3 30.7 1.0 CG S:GLU234 4.0 33.8 1.0 ND1 R:HIS190 4.1 32.3 1.0 CG R:HIS190 4.2 32.4 1.0 ND1 S:HIS266 4.2 31.7 1.0 ND1 S:HIS219 4.2 30.2 1.0 CG S:HIS219 4.3 30.7 1.0 CG S:HIS266 4.3 31.9 1.0 ND1 R:HIS230 4.3 30.4 1.0 CG R:HIS230 4.4 30.7 1.0 CG1 S:ILE223 4.4 31.5 1.0 CG2 R:VAL194 4.6 31.0 1.0 O S:HOH2033 4.8 39.5 1.0 CD1 S:ILE223 4.9 31.5 1.0 CB S:GLU234 4.9 34.0 1.0

H.L.Axelrod, E.C.Abresch, M.L.Paddock, M.Y.Okamura, G.Feher. Determination of the Binding Sites of the Proton Transfer Inhibitors CD2+ and ZN2+ in Bacterial Reaction Centers. Proc.Natl.Acad.Sci.Usa V. 97 1542 2000.
ISSN: ISSN 0027-8424
PubMed: 10677497
DOI: 10.1073/PNAS.97.4.1542