Iron in PDB 2i5n: 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique

The structure of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique, PDB code: 2i5n was solved by L.Li, D.Mustafi, Q.Fu, V.Tereshko, D.L.Chen, J.D.Tice, R.F.Ismagilov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.96
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	220.400, 220.400, 113.009, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19

The structure of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Iron atom in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique (pdb code 2i5n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique, PDB code: 2i5n:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:25.2 occ:1.00 FE C:HEC401 0.0 25.2 1.0 NA C:HEC401 2.0 26.0 1.0 NE2 C:HIS91 2.0 26.9 1.0 NC C:HEC401 2.1 23.5 1.0 NB C:HEC401 2.1 23.9 1.0 ND C:HEC401 2.1 23.9 1.0 SD C:MET74 2.2 24.5 1.0 CE1 C:HIS91 3.0 28.3 1.0 C4A C:HEC401 3.0 27.0 1.0 CD2 C:HIS91 3.0 26.5 1.0 C1B C:HEC401 3.1 23.9 1.0 C1D C:HEC401 3.1 25.2 1.0 C4C C:HEC401 3.1 25.2 1.0 C1A C:HEC401 3.1 29.0 1.0 C1C C:HEC401 3.1 25.8 1.0 C4B C:HEC401 3.1 23.3 1.0 C4D C:HEC401 3.1 26.1 1.0 CE C:MET74 3.4 26.2 1.0 CG C:MET74 3.4 20.8 1.0 CHB C:HEC401 3.4 26.1 1.0 CHD C:HEC401 3.4 24.7 1.0 CHC C:HEC401 3.5 24.6 1.0 CHA C:HEC401 3.5 25.6 1.0 ND1 C:HIS91 4.1 24.6 1.0 CG C:HIS91 4.2 26.8 1.0 CB C:MET74 4.2 23.0 1.0 C3A C:HEC401 4.3 29.7 1.0 C2A C:HEC401 4.3 29.0 1.0 C2D C:HEC401 4.3 26.8 1.0 C2B C:HEC401 4.3 23.8 1.0 C3D C:HEC401 4.3 25.0 1.0 C3C C:HEC401 4.3 23.5 1.0 C3B C:HEC401 4.3 24.5 1.0 C2C C:HEC401 4.3 24.5 1.0

Iron binding site 2 out of 5 in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe402 b:22.1 occ:1.00 FE C:HEC402 0.0 22.1 1.0 NB C:HEC402 2.0 21.3 1.0 NE2 C:HIS136 2.1 20.6 1.0 ND C:HEC402 2.1 23.6 1.0 NA C:HEC402 2.1 22.6 1.0 NC C:HEC402 2.1 20.2 1.0 SD C:MET110 2.2 23.7 1.0 CE1 C:HIS136 3.0 19.1 1.0 C1B C:HEC402 3.0 21.6 1.0 C4A C:HEC402 3.1 21.6 1.0 C4B C:HEC402 3.1 22.6 1.0 C1D C:HEC402 3.1 22.7 1.0 C1A C:HEC402 3.1 21.9 1.0 C4D C:HEC402 3.1 22.2 1.0 C1C C:HEC402 3.1 18.9 1.0 C4C C:HEC402 3.1 20.8 1.0 CD2 C:HIS136 3.1 18.5 1.0 CE C:MET110 3.3 22.4 1.0 CG C:MET110 3.4 23.8 1.0 CHB C:HEC402 3.4 20.8 1.0 CHC C:HEC402 3.4 20.7 1.0 CHD C:HEC402 3.4 21.3 1.0 CHA C:HEC402 3.5 22.4 1.0 ND1 C:HIS136 4.1 17.7 1.0 CB C:MET110 4.1 23.3 1.0 CG C:HIS136 4.2 20.0 1.0 C2B C:HEC402 4.3 20.6 1.0 C3B C:HEC402 4.3 20.9 1.0 C3A C:HEC402 4.3 23.6 1.0 C2A C:HEC402 4.3 23.3 1.0 C2D C:HEC402 4.3 24.0 1.0 C3D C:HEC402 4.3 26.1 1.0 C2C C:HEC402 4.3 20.0 1.0 C3C C:HEC402 4.3 18.9 1.0

Iron binding site 3 out of 5 in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe403 b:17.3 occ:1.00 FE C:HEC403 0.0 17.3 1.0 NB C:HEC403 2.0 16.5 1.0 NC C:HEC403 2.1 16.3 1.0 NE2 C:HIS248 2.1 17.2 1.0 NA C:HEC403 2.1 15.3 1.0 ND C:HEC403 2.1 16.2 1.0 SD C:MET233 2.2 16.7 1.0 CD2 C:HIS248 3.0 17.0 1.0 C4B C:HEC403 3.0 19.8 1.0 C1C C:HEC403 3.0 15.4 1.0 C1B C:HEC403 3.1 16.9 1.0 C4A C:HEC403 3.1 15.3 1.0 CE1 C:HIS248 3.1 16.4 1.0 C4C C:HEC403 3.1 15.2 1.0 C1D C:HEC403 3.1 18.8 1.0 C1A C:HEC403 3.1 16.0 1.0 C4D C:HEC403 3.1 18.7 1.0 CE C:MET233 3.3 16.6 1.0 CG C:MET233 3.4 18.2 1.0 CHC C:HEC403 3.4 16.9 1.0 CHB C:HEC403 3.4 16.4 1.0 CHD C:HEC403 3.5 17.3 1.0 CHA C:HEC403 3.5 16.6 1.0 ND1 C:HIS248 4.2 16.3 1.0 CG C:HIS248 4.2 18.0 1.0 CB C:MET233 4.2 18.8 1.0 C3B C:HEC403 4.3 18.1 1.0 C2B C:HEC403 4.3 16.4 1.0 C2C C:HEC403 4.3 18.1 1.0 C3A C:HEC403 4.3 18.6 1.0 C2D C:HEC403 4.3 16.4 1.0 C3C C:HEC403 4.3 15.6 1.0 C2A C:HEC403 4.3 17.6 1.0 C3D C:HEC403 4.3 18.8 1.0

Iron binding site 4 out of 5 in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe404 b:19.4 occ:1.00 FE C:HEC404 0.0 19.4 1.0 NE2 C:HIS124 2.0 23.2 1.0 NB C:HEC404 2.1 18.8 1.0 NE2 C:HIS309 2.1 18.1 1.0 ND C:HEC404 2.1 18.9 1.0 NA C:HEC404 2.1 16.7 1.0 NC C:HEC404 2.1 20.0 1.0 CE1 C:HIS309 2.9 20.5 1.0 CE1 C:HIS124 3.0 19.2 1.0 C1B C:HEC404 3.1 17.7 1.0 C4A C:HEC404 3.1 17.3 1.0 C1D C:HEC404 3.1 19.6 1.0 C4B C:HEC404 3.1 18.8 1.0 CD2 C:HIS124 3.1 19.9 1.0 C4D C:HEC404 3.1 18.8 1.0 C1C C:HEC404 3.1 19.6 1.0 C1A C:HEC404 3.1 17.3 1.0 C4C C:HEC404 3.1 20.5 1.0 CD2 C:HIS309 3.2 17.1 1.0 CHB C:HEC404 3.4 16.4 1.0 CHD C:HEC404 3.4 19.6 1.0 CHC C:HEC404 3.4 17.7 1.0 CHA C:HEC404 3.5 18.5 1.0 ND1 C:HIS124 4.1 20.7 1.0 ND1 C:HIS309 4.1 20.1 1.0 CG C:HIS124 4.2 20.7 1.0 CG C:HIS309 4.2 16.9 1.0 C2B C:HEC404 4.3 18.6 1.0 C3D C:HEC404 4.3 21.5 1.0 C3A C:HEC404 4.3 18.0 1.0 C2D C:HEC404 4.3 21.4 1.0 C3B C:HEC404 4.3 19.9 1.0 C2A C:HEC404 4.3 18.6 1.0 C2C C:HEC404 4.3 19.3 1.0 C3C C:HEC404 4.3 19.4 1.0 CD C:PRO315 4.8 21.5 1.0 CG C:PRO315 4.9 21.1 1.0

Iron binding site 5 out of 5 in the 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 1.96 A X-Ray Structure of Photosynthetic Reaction Center From Rhodopseudomonas Viridis:Crystals Grown By Microfluidic Technique within 5.0Å range: probe atom residue distance (Å) B Occ L:Fe500 b:16.4 occ:1.00 OE2 M:GLU232 2.1 18.1 1.0 NE2 L:HIS190 2.1 18.1 1.0 NE2 M:HIS217 2.1 15.4 1.0 NE2 L:HIS230 2.1 17.9 1.0 NE2 M:HIS264 2.1 17.2 1.0 OE1 M:GLU232 2.5 19.5 1.0 CD M:GLU232 2.6 17.6 1.0 CE1 L:HIS190 3.0 18.8 1.0 CE1 M:HIS217 3.0 14.7 1.0 CE1 L:HIS230 3.0 16.9 1.0 CE1 M:HIS264 3.1 18.2 1.0 CD2 L:HIS190 3.2 17.1 1.0 CD2 M:HIS217 3.2 15.2 1.0 CD2 M:HIS264 3.2 16.0 1.0 CD2 L:HIS230 3.2 15.6 1.0 CG M:GLU232 4.1 17.4 1.0 ND1 L:HIS190 4.1 18.8 1.0 ND1 M:HIS217 4.2 15.2 1.0 ND1 L:HIS230 4.2 14.6 1.0 ND1 M:HIS264 4.2 16.5 1.0 CG L:HIS190 4.3 17.6 1.0 CG M:HIS217 4.3 15.4 1.0 CG M:HIS264 4.3 16.2 1.0 CG L:HIS230 4.3 17.1 1.0 CG1 M:ILE221 4.5 16.5 1.0 CG1 L:ILE194 4.6 19.1 1.0 O M:HOH859 4.8 19.3 1.0

L.Li, D.Mustafi, Q.Fu, V.Tereshko, D.L.Chen, J.D.Tice, R.F.Ismagilov. Nanoliter Microfluidic Hybrid Method For Simultaneous Screening and Optimization Validated with Crystallization of Membrane Proteins. Proc.Natl.Acad.Sci.Usa V. 103 19243 2006.
ISSN: ISSN 0027-8424
PubMed: 17159147
DOI: 10.1073/PNAS.0607502103