Iron in PDB 1dv6: Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor ZN2+

The structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor ZN2+, PDB code: 1dv6 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)	27.52 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	141.517, 141.517, 278.506, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 26.5

The structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides in the Charge-Neutral Dqaqb State with the Proton Transfer Inhibitor ZN2+ also contains other interesting chemical elements:

Magnesium	(Mg)	8 atoms
Chlorine	(Cl)	2 atoms
Zinc	(Zn)	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 ZN2+ (pdb code 1dv6). 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 ZN2+, PDB code: 1dv6:
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 ZN2+


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 ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe1007 b:35.4 occ:1.00 NE2 L:HIS190 2.1 36.0 1.0 NE2 M:HIS266 2.1 33.6 1.0 NE2 M:HIS219 2.2 37.5 1.0 NE2 L:HIS230 2.2 33.7 1.0 OE2 M:GLU234 2.3 38.1 1.0 OE1 M:GLU234 2.4 37.1 1.0 CD M:GLU234 2.6 38.0 1.0 CE1 L:HIS190 3.0 35.9 1.0 CE1 M:HIS266 3.0 33.6 1.0 CE1 L:HIS230 3.1 34.0 1.0 CE1 M:HIS219 3.1 37.4 1.0 CD2 M:HIS219 3.2 36.3 1.0 CD2 L:HIS190 3.2 36.5 1.0 CD2 M:HIS266 3.2 34.6 1.0 CD2 L:HIS230 3.4 34.7 1.0 CG M:GLU234 4.1 37.3 1.0 ND1 L:HIS190 4.1 37.0 1.0 ND1 M:HIS266 4.2 33.7 1.0 CG L:HIS190 4.2 36.5 1.0 ND1 L:HIS230 4.3 33.9 1.0 CG M:HIS266 4.3 35.0 1.0 ND1 M:HIS219 4.3 37.9 1.0 CG M:HIS219 4.3 37.8 1.0 CG L:HIS230 4.4 35.9 1.0 CG1 M:ILE223 4.5 33.5 1.0 O M:HOH1026 4.6 42.3 1.0 CG2 L:VAL194 4.7 33.8 1.0 CD1 M:ILE223 5.0 32.3 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 ZN2+


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 ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ S:Fe2007 b:42.1 occ:1.00 NE2 R:HIS190 2.0 39.3 1.0 NE2 S:HIS219 2.2 39.5 1.0 NE2 R:HIS230 2.2 39.0 1.0 NE2 S:HIS266 2.2 37.6 1.0 OE2 S:GLU234 2.2 40.4 1.0 OE1 S:GLU234 2.3 42.2 1.0 CD S:GLU234 2.6 41.2 1.0 CE1 R:HIS190 2.9 39.1 1.0 CE1 R:HIS230 3.0 40.2 1.0 CE1 S:HIS266 3.0 38.6 1.0 CE1 S:HIS219 3.1 40.1 1.0 CD2 R:HIS190 3.2 39.1 1.0 CD2 S:HIS219 3.2 40.0 1.0 CD2 R:HIS230 3.3 39.0 1.0 CD2 S:HIS266 3.3 38.8 1.0 CG S:GLU234 4.1 40.4 1.0 ND1 R:HIS190 4.1 40.3 1.0 ND1 R:HIS230 4.2 38.7 1.0 CG R:HIS190 4.2 39.6 1.0 ND1 S:HIS266 4.2 38.6 1.0 ND1 S:HIS219 4.3 40.5 1.0 CG S:HIS219 4.3 40.8 1.0 CG R:HIS230 4.3 39.0 1.0 CG S:HIS266 4.4 38.9 1.0 CG1 S:ILE223 4.5 35.1 1.0 CG2 R:VAL194 4.8 38.3 1.0 O R:HOH2052 4.8 73.4 1.0 CD1 S:ILE223 4.9 35.2 1.0 CB S:GLU234 5.0 40.3 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