Iron in PDB 7r0w: 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules

The structure of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Iron atom in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules (pdb code 7r0w). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules, PDB code: 7r0w:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe301 b:89.8 occ:1.00 FE I:HEM301 0.0 89.8 1.0 NB I:HEM301 2.0 57.9 1.0 ND I:HEM301 2.0 53.0 1.0 NC I:HEM301 2.0 46.9 1.0 NA I:HEM301 2.0 65.5 1.0 NE2 I:HIS93 2.2 51.3 1.0 NE2 I:HIS194 2.4 39.4 1.0 C4B I:HEM301 3.0 52.5 1.0 C4D I:HEM301 3.0 40.0 1.0 C1A I:HEM301 3.1 53.8 1.0 C1C I:HEM301 3.1 47.0 1.0 C1B I:HEM301 3.1 38.8 1.0 C1D I:HEM301 3.1 45.1 1.0 C4C I:HEM301 3.1 52.0 1.0 C4A I:HEM301 3.1 49.2 1.0 CD2 I:HIS93 3.1 42.2 1.0 CE1 I:HIS93 3.2 54.0 1.0 CE1 I:HIS194 3.3 47.3 1.0 CHC I:HEM301 3.4 47.0 1.0 CHA I:HEM301 3.4 46.3 1.0 CD2 I:HIS194 3.4 38.8 1.0 CHB I:HEM301 3.5 31.0 1.0 CHD I:HEM301 3.5 50.5 1.0 ND1 I:HIS93 4.2 44.5 1.0 CG I:HIS93 4.2 38.1 1.0 C3D I:HEM301 4.3 34.8 1.0 C3B I:HEM301 4.3 44.2 1.0 C2A I:HEM301 4.3 39.2 1.0 C2D I:HEM301 4.3 32.9 1.0 C2C I:HEM301 4.3 42.8 1.0 C2B I:HEM301 4.3 48.4 1.0 C3A I:HEM301 4.3 43.6 1.0 C3C I:HEM301 4.3 43.4 1.0 NE2 I:GLN54 4.5 61.7 1.0 ND1 I:HIS194 4.5 38.7 1.0 CG I:HIS194 4.6 42.3 1.0 CE I:MET61 4.8 55.1 1.0

Iron binding site 2 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe302 b:107.5 occ:1.00 FE I:HEM302 0.0 107.5 1.0 O I:HOH401 2.0 58.7 1.0 NA I:HEM302 2.0 63.0 1.0 NC I:HEM302 2.0 59.1 1.0 ND I:HEM302 2.0 62.1 1.0 NB I:HEM302 2.1 67.6 1.0 C1B I:HEM302 3.0 56.3 1.0 C4B I:HEM302 3.1 60.1 1.0 C4C I:HEM302 3.1 54.2 1.0 C1A I:HEM302 3.1 64.1 1.0 C4A I:HEM302 3.1 59.5 1.0 C1C I:HEM302 3.1 54.8 1.0 C4D I:HEM302 3.1 59.5 1.0 C1D I:HEM302 3.1 54.0 1.0 CZ J:PHE40 3.3 62.5 1.0 CHB I:HEM302 3.4 59.0 1.0 CHD I:HEM302 3.4 55.0 1.0 CHA I:HEM302 3.4 61.7 1.0 CHC I:HEM302 3.4 58.4 1.0 CE2 J:PHE40 3.4 58.5 1.0 CE1 J:PHE40 4.0 63.5 1.0 O2A I:HEM303 4.1 69.5 1.0 C2B I:HEM302 4.2 62.6 1.0 C3B I:HEM302 4.2 57.8 1.0 C3C I:HEM302 4.3 57.1 1.0 C2A I:HEM302 4.3 61.4 1.0 C2C I:HEM302 4.3 53.3 1.0 C3A I:HEM302 4.3 58.0 1.0 C2D I:HEM302 4.3 46.5 1.0 C3D I:HEM302 4.3 60.9 1.0 CD2 J:PHE40 4.3 58.1 1.0 CA I:GLY45 4.4 44.5 1.0 O I:TYR41 4.6 65.6 1.0 CMA I:HEM303 4.6 49.9 1.0 N I:GLY45 4.7 44.7 1.0 CD1 J:PHE40 4.8 68.7 1.0 CG J:PHE40 4.9 65.5 1.0 CAA I:HEM303 4.9 46.7 1.0

Iron binding site 3 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe303 b:69.6 occ:1.00 FE I:HEM303 0.0 69.6 1.0 NB I:HEM303 2.0 53.0 1.0 NC I:HEM303 2.0 52.8 1.0 ND I:HEM303 2.1 42.9 1.0 NA I:HEM303 2.1 39.8 1.0 NE2 I:HIS107 2.2 55.1 1.0 NE2 I:HIS209 2.6 47.4 1.0 CD2 I:HIS107 2.9 27.3 1.0 C1C I:HEM303 3.0 42.6 1.0 C4C I:HEM303 3.0 44.6 1.0 C4B I:HEM303 3.0 52.1 1.0 C1B I:HEM303 3.1 38.3 1.0 C4A I:HEM303 3.1 39.7 1.0 C4D I:HEM303 3.1 45.6 1.0 C1A I:HEM303 3.1 37.8 1.0 C1D I:HEM303 3.1 37.6 1.0 CE1 I:HIS107 3.3 59.4 1.0 CE1 I:HIS209 3.3 47.1 1.0 CHC I:HEM303 3.4 46.7 1.0 CHD I:HEM303 3.4 41.1 1.0 CHB I:HEM303 3.4 50.8 1.0 CHA I:HEM303 3.4 44.2 1.0 CD2 I:HIS209 3.5 29.0 1.0 CG I:HIS107 4.1 40.4 1.0 C2C I:HEM303 4.2 37.6 1.0 C3C I:HEM303 4.2 44.2 1.0 ND1 I:HIS107 4.2 63.5 1.0 C3B I:HEM303 4.3 39.7 1.0 C2B I:HEM303 4.3 18.6 1.0 C3A I:HEM303 4.3 33.4 1.0 C3D I:HEM303 4.3 37.0 1.0 C2A I:HEM303 4.3 34.0 1.0 C2D I:HEM303 4.3 24.9 1.0 ND1 I:HIS209 4.4 50.6 1.0 CG I:HIS209 4.5 33.9 1.0

Iron binding site 4 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ K:Fe301 b:104.3 occ:1.00 FE K:HEC301 0.0 104.3 1.0 NC K:HEC301 2.0 100.0 1.0 NA K:HEC301 2.1 96.8 1.0 NB K:HEC301 2.1 99.3 1.0 ND K:HEC301 2.1 98.0 1.0 NE2 K:HIS26 2.6 92.8 1.0 N K:TYR1 2.9 103.7 1.0 C1C K:HEC301 3.0 100.6 1.0 C1A K:HEC301 3.1 98.3 1.0 C4D K:HEC301 3.1 97.8 1.0 C1B K:HEC301 3.1 98.0 1.0 C4A K:HEC301 3.1 97.6 1.0 C4C K:HEC301 3.1 98.5 1.0 C1D K:HEC301 3.1 97.6 1.0 C4B K:HEC301 3.1 98.9 1.0 O K:TYR1 3.2 101.7 1.0 CA K:TYR1 3.3 99.6 1.0 CD2 K:HIS26 3.3 92.2 1.0 CHC K:HEC301 3.4 101.6 1.0 C K:TYR1 3.4 100.1 1.0 CHA K:HEC301 3.4 98.3 1.0 CHB K:HEC301 3.5 97.4 1.0 CHD K:HEC301 3.5 97.9 1.0 CE1 K:HIS26 3.6 97.2 1.0 C2C K:HEC301 4.3 101.8 1.0 C2A K:HEC301 4.3 99.5 1.0 C2B K:HEC301 4.3 97.9 1.0 C3C K:HEC301 4.3 99.1 1.0 C3A K:HEC301 4.3 98.5 1.0 C3D K:HEC301 4.3 98.3 1.0 C2D K:HEC301 4.3 99.5 1.0 C3B K:HEC301 4.3 96.0 1.0 N K:PRO2 4.4 94.0 1.0 CG K:HIS26 4.6 94.3 1.0 ND1 K:HIS26 4.7 97.3 1.0 CB K:TYR1 4.8 98.9 1.0 CE3 K:TRP4 5.0 99.6 1.0

Iron binding site 5 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:75.4 occ:1.00 FE A:HEM301 0.0 75.4 1.0 NB A:HEM301 2.0 49.5 1.0 NC A:HEM301 2.0 47.7 1.0 NA A:HEM301 2.0 40.6 1.0 ND A:HEM301 2.1 46.2 1.0 NE2 A:HIS107 2.2 57.5 1.0 NE2 A:HIS209 2.6 46.1 1.0 CD2 A:HIS107 2.9 34.1 1.0 C1C A:HEM301 3.0 49.2 1.0 C4C A:HEM301 3.0 37.6 1.0 C4B A:HEM301 3.0 49.2 1.0 C1B A:HEM301 3.0 45.7 1.0 C4A A:HEM301 3.1 43.4 1.0 C1D A:HEM301 3.1 39.4 1.0 C1A A:HEM301 3.1 31.0 1.0 C4D A:HEM301 3.1 42.8 1.0 CE1 A:HIS107 3.2 53.2 1.0 CE1 A:HIS209 3.4 42.4 1.0 CHC A:HEM301 3.4 47.4 1.0 CHD A:HEM301 3.4 41.6 1.0 CHB A:HEM301 3.4 56.8 1.0 CHA A:HEM301 3.4 41.5 1.0 CD2 A:HIS209 3.5 31.6 1.0 CG A:HIS107 4.1 45.1 1.0 C2C A:HEM301 4.2 47.2 1.0 C3C A:HEM301 4.2 39.8 1.0 ND1 A:HIS107 4.2 53.5 1.0 C3B A:HEM301 4.2 41.8 1.0 C2B A:HEM301 4.2 34.0 1.0 C3A A:HEM301 4.3 40.4 1.0 C3D A:HEM301 4.3 39.4 1.0 C2D A:HEM301 4.3 36.0 1.0 C2A A:HEM301 4.3 30.8 1.0 ND1 A:HIS209 4.4 56.5 1.0 CG A:HIS209 4.5 40.2 1.0

Iron binding site 6 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe302 b:88.2 occ:1.00 FE A:HEM302 0.0 88.2 1.0 ND A:HEM302 2.0 67.3 1.0 NB A:HEM302 2.0 66.7 1.0 NA A:HEM302 2.0 56.9 1.0 NC A:HEM302 2.0 48.3 1.0 NE2 A:HIS194 2.2 57.9 1.0 NE2 A:HIS93 2.5 56.6 1.0 C4D A:HEM302 3.0 55.3 1.0 C1A A:HEM302 3.0 54.0 1.0 C4B A:HEM302 3.0 57.5 1.0 CE1 A:HIS194 3.0 55.7 1.0 C1D A:HEM302 3.1 55.3 1.0 C4A A:HEM302 3.1 53.5 1.0 C1B A:HEM302 3.1 54.6 1.0 C1C A:HEM302 3.1 45.6 1.0 C4C A:HEM302 3.1 57.3 1.0 CD2 A:HIS194 3.3 60.4 1.0 CD2 A:HIS93 3.3 60.0 1.0 CE1 A:HIS93 3.4 60.6 1.0 CHA A:HEM302 3.4 54.0 1.0 CHC A:HEM302 3.4 49.8 1.0 CHB A:HEM302 3.4 47.1 1.0 CHD A:HEM302 3.4 56.2 1.0 ND1 A:HIS194 4.2 56.3 1.0 C3D A:HEM302 4.3 52.6 1.0 C2D A:HEM302 4.3 50.5 1.0 C2A A:HEM302 4.3 52.2 1.0 C3A A:HEM302 4.3 54.4 1.0 C3B A:HEM302 4.3 51.2 1.0 C2B A:HEM302 4.3 53.6 1.0 C2C A:HEM302 4.3 53.7 1.0 C3C A:HEM302 4.3 54.5 1.0 CG A:HIS194 4.4 56.9 1.0 ND1 A:HIS93 4.4 63.2 1.0 CG A:HIS93 4.4 60.3 1.0 NE2 A:GLN54 4.6 58.5 1.0

Iron binding site 7 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:103.8 occ:1.00 FE B:HEM301 0.0 103.8 1.0 O B:HOH401 1.9 63.5 1.0 ND B:HEM301 2.0 57.9 1.0 NC B:HEM301 2.0 66.8 1.0 NA B:HEM301 2.0 61.9 1.0 NB B:HEM301 2.1 70.6 1.0 C4B B:HEM301 3.0 58.1 1.0 C4D B:HEM301 3.0 59.2 1.0 C1A B:HEM301 3.0 61.9 1.0 C1B B:HEM301 3.1 57.8 1.0 C1D B:HEM301 3.1 50.5 1.0 C4C B:HEM301 3.1 60.6 1.0 C1C B:HEM301 3.1 60.1 1.0 C4A B:HEM301 3.1 49.4 1.0 CZ B:PHE40 3.3 62.8 1.0 CHA B:HEM301 3.4 62.4 1.0 CHC B:HEM301 3.4 54.5 1.0 CHD B:HEM301 3.4 56.0 1.0 CHB B:HEM301 3.4 51.5 1.0 CE2 B:PHE40 3.6 62.3 1.0 CE1 B:PHE40 4.0 59.6 1.0 O1A A:HEM301 4.2 65.8 1.0 C3B B:HEM301 4.2 61.8 1.0 C2B B:HEM301 4.2 61.9 1.0 C2A B:HEM301 4.3 61.2 1.0 C3D B:HEM301 4.3 56.1 1.0 C2D B:HEM301 4.3 51.2 1.0 C3A B:HEM301 4.3 49.8 1.0 C3C B:HEM301 4.3 59.7 1.0 C2C B:HEM301 4.3 59.6 1.0 CMA A:HEM301 4.4 57.0 1.0 CD2 B:PHE40 4.5 59.3 1.0 CA A:GLY45 4.5 44.4 1.0 CAA A:HEM301 4.8 49.7 1.0 O A:TYR41 4.8 71.6 1.0 CBA A:HEM301 4.8 50.7 1.0 CD1 B:PHE40 4.8 63.2 1.0 N A:GLY45 4.9 48.3 1.0 CGA A:HEM301 5.0 53.2 1.0

Iron binding site 8 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe302 b:116.4 occ:1.00 FE C:HEC302 0.0 116.4 1.0 NA C:HEC302 2.0 106.3 1.0 NC C:HEC302 2.0 105.1 1.0 NB C:HEC302 2.1 103.7 1.0 ND C:HEC302 2.1 107.6 1.0 NE2 C:HIS26 2.4 101.6 1.0 N C:TYR1 2.7 105.5 1.0 C4A C:HEC302 3.0 105.3 1.0 C1C C:HEC302 3.1 107.2 1.0 C1A C:HEC302 3.1 102.8 1.0 C1B C:HEC302 3.1 102.3 1.0 C4C C:HEC302 3.1 103.9 1.0 C1D C:HEC302 3.1 104.5 1.0 CA C:TYR1 3.1 104.5 1.0 C4D C:HEC302 3.1 107.2 1.0 C4B C:HEC302 3.1 102.8 1.0 CE1 C:HIS26 3.2 102.8 1.0 O C:TYR1 3.3 104.3 1.0 C C:TYR1 3.4 105.4 1.0 CHB C:HEC302 3.4 105.9 1.0 CHD C:HEC302 3.4 102.8 1.0 CHA C:HEC302 3.5 103.2 1.0 CHC C:HEC302 3.5 107.5 1.0 CD2 C:HIS26 3.5 103.0 1.0 C3A C:HEC302 4.3 104.8 1.0 C2A C:HEC302 4.3 102.9 1.0 C2C C:HEC302 4.3 108.1 1.0 N C:PRO2 4.3 102.2 1.0 C3C C:HEC302 4.3 107.3 1.0 C2B C:HEC302 4.3 100.7 1.0 C2D C:HEC302 4.3 104.0 1.0 C3B C:HEC302 4.3 101.4 1.0 C3D C:HEC302 4.3 105.2 1.0 ND1 C:HIS26 4.4 100.7 1.0 CG C:HIS26 4.6 100.3 1.0 CB C:TYR1 4.6 104.0 1.0 ND2 C:ASN154 4.7 105.9 1.0 CD C:PRO2 5.0 101.3 1.0

Iron binding site 9 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:168.9 occ:1.00 FE1 D:FES201 0.0 168.9 1.0 S1 D:FES201 2.2 167.2 1.0 S2 D:FES201 2.2 164.0 1.0 SG D:CYS138 2.5 140.4 1.0 FE2 D:FES201 2.7 179.2 1.0 SG D:CYS120 2.8 132.7 1.0 CB D:CYS120 3.2 127.3 1.0 CB D:CYS138 3.2 131.0 1.0 CB D:CYS140 3.7 136.2 1.0 CB D:CYS125 4.1 127.3 1.0 N D:HIS141 4.1 129.2 1.0 ND1 D:HIS141 4.2 131.7 1.0 O D:CYS125 4.3 124.7 1.0 CB D:SER143 4.4 134.5 1.0 CA D:CYS140 4.7 132.9 1.0 CA D:CYS138 4.7 130.7 1.0 N D:CYS140 4.7 132.0 1.0 CA D:CYS120 4.7 127.1 1.0 SG D:CYS140 4.7 147.6 1.0 N D:SER143 4.7 137.2 1.0 CB D:HIS122 4.8 127.8 1.0 CG1 D:VAL127 4.8 122.8 1.0 CD2 D:HIS122 4.8 131.1 1.0 C D:CYS140 4.9 134.0 1.0 CB D:HIS141 4.9 125.0 1.0 N D:CYS125 4.9 126.0 1.0 CA D:CYS125 4.9 123.8 1.0 N D:GLY142 4.9 144.3 1.0 CA D:HIS141 4.9 128.4 1.0 CG D:HIS141 5.0 125.8 1.0

Iron binding site 10 out of 12 in the 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of 2.8 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F-Petp Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Lipids and Plastoquinone Molecules within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:179.2 occ:1.00 FE2 D:FES201 0.0 179.2 1.0 S1 D:FES201 2.2 167.2 1.0 S2 D:FES201 2.2 164.0 1.0 CD2 D:HIS122 2.4 131.1 1.0 ND1 D:HIS141 2.5 131.7 1.0 CG D:HIS122 2.6 130.6 1.0 FE1 D:FES201 2.7 168.9 1.0 CB D:HIS122 3.0 127.8 1.0 CG D:HIS141 3.3 125.8 1.0 NE2 D:HIS122 3.3 130.1 1.0 CB D:HIS141 3.4 125.0 1.0 CE1 D:HIS141 3.5 129.0 1.0 ND1 D:HIS122 3.6 129.9 1.0 SG D:CYS120 3.6 132.7 1.0 CE1 D:HIS122 3.9 129.1 1.0 N D:HIS141 4.1 129.2 1.0 CA D:HIS122 4.3 127.5 1.0 CA D:HIS141 4.3 128.4 1.0 N D:LEU123 4.4 116.8 1.0 CD2 D:HIS141 4.4 124.4 1.0 CG D:PRO155 4.4 134.0 1.0 NE2 D:HIS141 4.5 126.7 1.0 CB D:CYS140 4.6 136.2 1.0 C D:HIS122 4.6 126.6 1.0 N D:HIS122 4.8 128.1 1.0 CB D:CYS120 4.8 127.3 1.0 CB D:SER143 4.9 134.5 1.0 C D:HIS141 4.9 129.0 1.0 SG D:CYS140 4.9 147.6 1.0 C D:CYS140 4.9 134.0 1.0 CB D:LEU123 5.0 115.9 1.0

M.S.Proctor, L.A.Malone, D.A.Farmer, D.J.K.Swainsbury, F.R.Hawkings, F.Pastorelli, T.Z.Emrich-Mills, C.A.Siebert, C.N.Hunter, M.P.Johnson, A.Hitchcock. Cryo-Em Structures of the Synechocystis Sp. Pcc 6803 Cytochrome B6F Complex with and Without the Regulatory Petp Subunit. Biochem.J. V. 479 1487 2022.
ISSN: ESSN 1470-8728
PubMed: 35726684
DOI: 10.1042/BCJ20220124