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Iron in PDB 7zxy: 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.

Enzymatic activity of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.

All present enzymatic activity of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.:
7.1.1.6;

Other elements in 7zxy:

The structure of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Iron Binding Sites:

Pages:

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

Binding sites:

The binding sites of Iron atom in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. (pdb code 7zxy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules., PDB code: 7zxy:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in 7zxy

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Iron binding site 1 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe302

b:1.3
occ:1.00
FE A:HEM302 0.0 1.3 1.0
NE2 A:HIS93 1.7 1.6 1.0
NB A:HEM302 2.0 1.3 1.0
NA A:HEM302 2.1 1.3 1.0
NC A:HEM302 2.1 1.3 1.0
ND A:HEM302 2.1 1.3 1.0
CE1 A:HIS93 2.4 1.6 1.0
NE2 A:HIS194 2.5 1.3 1.0
CD2 A:HIS93 3.0 1.6 1.0
C4B A:HEM302 3.0 1.3 1.0
C1B A:HEM302 3.0 1.3 1.0
C1D A:HEM302 3.1 1.3 1.0
C4D A:HEM302 3.1 1.3 1.0
C1C A:HEM302 3.1 1.3 1.0
C1A A:HEM302 3.1 1.3 1.0
C4A A:HEM302 3.1 1.3 1.0
C4C A:HEM302 3.1 1.3 1.0
CD2 A:HIS194 3.3 1.3 1.0
CHC A:HEM302 3.4 1.3 1.0
CHB A:HEM302 3.4 1.3 1.0
CHA A:HEM302 3.4 1.3 1.0
CHD A:HEM302 3.4 1.3 1.0
CE1 A:HIS194 3.5 1.3 1.0
ND1 A:HIS93 3.6 1.6 1.0
CG A:HIS93 3.9 1.6 1.0
C3B A:HEM302 4.2 1.3 1.0
C2D A:HEM302 4.2 1.3 1.0
C2B A:HEM302 4.2 1.3 1.0
C3D A:HEM302 4.3 1.3 1.0
C2A A:HEM302 4.3 1.3 1.0
C3A A:HEM302 4.3 1.3 1.0
C2C A:HEM302 4.3 1.3 1.0
C3C A:HEM302 4.3 1.3 1.0
CE2 A:PHE138 4.5 0.1 1.0
CG A:HIS194 4.5 1.3 1.0
OE1 A:GLN54 4.6 2.7 1.0
ND1 A:HIS194 4.6 1.3 1.0
CE A:MET61 4.7 3.6 1.0
CA A:GLY58 4.9 5.2 1.0

Iron binding site 2 out of 12 in 7zxy

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Iron binding site 2 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe303

b:1.2
occ:1.00
FE A:HEM303 0.0 1.2 1.0
NE2 A:HIS107 2.0 1.7 1.0
ND A:HEM303 2.0 1.2 1.0
NA A:HEM303 2.0 1.2 1.0
NB A:HEM303 2.0 1.2 1.0
NC A:HEM303 2.1 1.2 1.0
NE2 A:HIS209 2.2 1.8 1.0
CD2 A:HIS107 2.9 1.7 1.0
C1C A:HEM303 3.0 1.2 1.0
C4C A:HEM303 3.0 1.2 1.0
CD2 A:HIS209 3.0 1.8 1.0
C4D A:HEM303 3.0 1.2 1.0
C4B A:HEM303 3.0 1.2 1.0
C1D A:HEM303 3.0 1.2 1.0
C1B A:HEM303 3.1 1.2 1.0
C4A A:HEM303 3.1 1.2 1.0
C1A A:HEM303 3.1 1.2 1.0
CE1 A:HIS107 3.1 1.7 1.0
CE1 A:HIS209 3.3 1.8 1.0
CHC A:HEM303 3.4 1.2 1.0
CHD A:HEM303 3.4 1.2 1.0
CHA A:HEM303 3.4 1.2 1.0
CHB A:HEM303 3.4 1.2 1.0
CG A:HIS107 4.1 1.7 1.0
ND1 A:HIS107 4.2 1.7 1.0
C2C A:HEM303 4.2 1.2 1.0
C3C A:HEM303 4.2 1.2 1.0
CG A:HIS209 4.2 1.8 1.0
C3D A:HEM303 4.2 1.2 1.0
C2D A:HEM303 4.3 1.2 1.0
C2B A:HEM303 4.3 1.2 1.0
C3B A:HEM303 4.3 1.2 1.0
C3A A:HEM303 4.3 1.2 1.0
C2A A:HEM303 4.3 1.2 1.0
ND1 A:HIS209 4.3 1.8 1.0
CD1 A:ILE213 4.9 2.7 1.0

Iron binding site 3 out of 12 in 7zxy

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Iron binding site 3 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe304

b:4.2
occ:1.00
FE A:HEC304 0.0 4.2 1.0
ND A:HEC304 2.0 4.2 1.0
NA A:HEC304 2.0 4.2 1.0
NC A:HEC304 2.0 4.2 1.0
NB A:HEC304 2.0 4.2 1.0
C1C A:HEC304 3.0 4.2 1.0
C4B A:HEC304 3.0 4.2 1.0
C4D A:HEC304 3.1 4.2 1.0
C1B A:HEC304 3.1 4.2 1.0
C1D A:HEC304 3.1 4.2 1.0
C4A A:HEC304 3.1 4.2 1.0
C1A A:HEC304 3.1 4.2 1.0
C4C A:HEC304 3.1 4.2 1.0
CZ B:PHE40 3.2 6.2 1.0
CHC A:HEC304 3.4 4.2 1.0
CHA A:HEC304 3.4 4.2 1.0
CHB A:HEC304 3.4 4.2 1.0
CHD A:HEC304 3.4 4.2 1.0
CE1 B:PHE40 3.8 6.2 1.0
CE2 B:PHE40 3.8 6.2 1.0
O1A A:HEM303 4.0 1.2 1.0
C2B A:HEC304 4.3 4.2 1.0
C3B A:HEC304 4.3 4.2 1.0
C3D A:HEC304 4.3 4.2 1.0
C2C A:HEC304 4.3 4.2 1.0
C2D A:HEC304 4.3 4.2 1.0
C3A A:HEC304 4.3 4.2 1.0
C2A A:HEC304 4.3 4.2 1.0
C3C A:HEC304 4.3 4.2 1.0
O A:TYR41 4.3 3.5 1.0
CMA A:HEM303 4.5 1.2 1.0
CD1 B:PHE40 4.7 6.2 1.0
CD2 B:PHE40 4.7 6.2 1.0
CA A:GLY45 4.7 2.4 1.0
N A:GLY45 4.9 2.4 1.0
CGA A:HEM303 4.9 1.2 1.0

Iron binding site 4 out of 12 in 7zxy

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Iron binding site 4 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe301

b:24.5
occ:1.00
FE C:HEC301 0.0 24.5 1.0
NC C:HEC301 2.0 24.5 1.0
NA C:HEC301 2.0 24.5 1.0
NB C:HEC301 2.1 24.5 1.0
ND C:HEC301 2.1 24.5 1.0
NE2 C:HIS26 2.3 21.1 1.0
N C:TYR1 2.7 24.0 1.0
CE1 C:HIS26 3.0 21.1 1.0
C4C C:HEC301 3.1 24.5 1.0
C1A C:HEC301 3.1 24.5 1.0
C4B C:HEC301 3.1 24.5 1.0
C1C C:HEC301 3.1 24.5 1.0
C1D C:HEC301 3.1 24.5 1.0
C4D C:HEC301 3.1 24.5 1.0
C4A C:HEC301 3.1 24.5 1.0
C1B C:HEC301 3.1 24.5 1.0
CD2 C:HIS26 3.4 21.1 1.0
CHD C:HEC301 3.4 24.5 1.0
CHA C:HEC301 3.4 24.5 1.0
CHC C:HEC301 3.4 24.5 1.0
CHB C:HEC301 3.5 24.5 1.0
CA C:TYR1 3.6 24.0 1.0
ND1 C:HIS26 4.1 21.1 1.0
C C:TYR1 4.2 24.0 1.0
C3C C:HEC301 4.3 24.5 1.0
C3B C:HEC301 4.3 24.5 1.0
C2A C:HEC301 4.3 24.5 1.0
C2C C:HEC301 4.3 24.5 1.0
C3A C:HEC301 4.3 24.5 1.0
C2B C:HEC301 4.3 24.5 1.0
CG C:HIS26 4.3 21.1 1.0
C3D C:HEC301 4.3 24.5 1.0
O C:TYR1 4.3 24.0 1.0
C2D C:HEC301 4.3 24.5 1.0
OD1 C:ASN154 4.6 19.5 1.0
CB C:TYR1 4.9 24.0 1.0
N C:GLY158 4.9 25.0 1.0
CA C:GLY158 5.0 25.0 1.0

Iron binding site 5 out of 12 in 7zxy

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Iron binding site 5 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:59.9
occ:1.00
FE1 D:FES201 0.0 59.9 1.0
ND1 D:HIS122 2.1 37.0 1.0
S1 D:FES201 2.2 59.9 1.0
S2 D:FES201 2.2 59.9 1.0
FE2 D:FES201 2.7 59.9 1.0
ND1 D:HIS141 2.9 36.1 1.0
CG D:HIS122 3.0 37.0 1.0
CB D:HIS122 3.2 37.0 1.0
CE1 D:HIS122 3.2 37.0 1.0
CE1 D:HIS141 3.3 36.1 1.0
N D:LEU123 3.6 35.4 1.0
CB D:LEU123 3.9 35.4 1.0
CG D:LEU123 4.0 35.4 1.0
CG D:HIS141 4.1 36.1 1.0
SG D:CYS138 4.1 33.1 1.0
CD2 D:HIS122 4.1 37.0 1.0
C D:HIS122 4.2 37.0 1.0
CA D:HIS122 4.2 37.0 1.0
NE2 D:HIS122 4.2 37.0 1.0
CB D:CYS140 4.2 38.0 1.0
SG D:CYS125 4.3 28.5 1.0
SG D:CYS120 4.4 30.8 1.0
CA D:LEU123 4.4 35.4 1.0
CD1 D:LEU123 4.5 35.4 1.0
NE2 D:HIS141 4.6 36.1 1.0
CB D:HIS141 4.6 36.1 1.0
OG D:SER143 4.7 34.1 1.0
N D:HIS122 4.8 37.0 1.0
N D:HIS141 4.8 36.1 1.0
CB D:CYS125 4.9 28.5 1.0
CB D:CYS120 4.9 30.8 1.0
CD2 D:HIS141 5.0 36.1 1.0
N D:GLY124 5.0 28.5 1.0

Iron binding site 6 out of 12 in 7zxy

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Iron binding site 6 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:59.9
occ:1.00
FE2 D:FES201 0.0 59.9 1.0
SG D:CYS138 2.2 33.1 1.0
S2 D:FES201 2.2 59.9 1.0
S1 D:FES201 2.2 59.9 1.0
SG D:CYS120 2.6 30.8 1.0
FE1 D:FES201 2.7 59.9 1.0
CB D:CYS138 2.9 33.1 1.0
OG D:SER143 3.4 34.1 1.0
CB D:CYS120 3.5 30.8 1.0
CB D:SER143 3.5 34.1 1.0
CB D:HIS122 3.9 37.0 1.0
ND1 D:HIS122 4.2 37.0 1.0
CA D:CYS138 4.4 33.1 1.0
CG D:HIS122 4.5 37.0 1.0
N D:SER143 4.6 34.1 1.0
CG1 D:VAL127 4.6 24.5 1.0
CA D:SER143 4.6 34.1 1.0
ND1 D:HIS141 4.7 36.1 1.0
OH D:TYR145 4.7 33.1 1.0
CB D:CYS125 4.8 28.5 1.0
N D:HIS122 4.9 37.0 1.0
CA D:CYS120 5.0 30.8 1.0
CA D:HIS122 5.0 37.0 1.0

Iron binding site 7 out of 12 in 7zxy

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Iron binding site 7 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe303

b:18.3
occ:1.00
FE I:HEM303 0.0 18.3 1.0
NE2 I:HIS194 1.7 4.9 1.0
NB I:HEM303 2.0 18.3 1.0
ND I:HEM303 2.0 18.3 1.0
NA I:HEM303 2.0 18.3 1.0
NC I:HEM303 2.0 18.3 1.0
NE2 I:HIS93 2.1 5.0 1.0
CE1 I:HIS194 2.6 4.9 1.0
CD2 I:HIS194 2.8 4.9 1.0
CE1 I:HIS93 2.9 5.0 1.0
C1D I:HEM303 3.0 18.3 1.0
C4D I:HEM303 3.0 18.3 1.0
C4B I:HEM303 3.1 18.3 1.0
C1A I:HEM303 3.1 18.3 1.0
C1B I:HEM303 3.1 18.3 1.0
C1C I:HEM303 3.1 18.3 1.0
C4C I:HEM303 3.1 18.3 1.0
C4A I:HEM303 3.1 18.3 1.0
CD2 I:HIS93 3.2 5.0 1.0
CHA I:HEM303 3.4 18.3 1.0
CHC I:HEM303 3.4 18.3 1.0
CHD I:HEM303 3.4 18.3 1.0
CHB I:HEM303 3.4 18.3 1.0
ND1 I:HIS194 3.8 4.9 1.0
CG I:HIS194 3.9 4.9 1.0
ND1 I:HIS93 4.1 5.0 1.0
C2D I:HEM303 4.2 18.3 1.0
C3D I:HEM303 4.3 18.3 1.0
C2A I:HEM303 4.3 18.3 1.0
C3B I:HEM303 4.3 18.3 1.0
C2B I:HEM303 4.3 18.3 1.0
CG I:HIS93 4.3 5.0 1.0
C3A I:HEM303 4.3 18.3 1.0
C2C I:HEM303 4.3 18.3 1.0
C3C I:HEM303 4.3 18.3 1.0
OE1 I:GLN54 4.8 5.5 1.0

Iron binding site 8 out of 12 in 7zxy

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Iron binding site 8 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe304

b:1.5
occ:1.00
FE I:HEM304 0.0 1.5 1.0
NB I:HEM304 2.0 1.5 1.0
NA I:HEM304 2.0 1.5 1.0
ND I:HEM304 2.0 1.5 1.0
NC I:HEM304 2.1 1.5 1.0
NE2 I:HIS107 2.1 1.8 1.0
NE2 I:HIS209 2.2 1.7 1.0
CD2 I:HIS107 2.8 1.8 1.0
CE1 I:HIS209 2.9 1.7 1.0
C1C I:HEM304 3.0 1.5 1.0
C4C I:HEM304 3.0 1.5 1.0
C4D I:HEM304 3.1 1.5 1.0
C4B I:HEM304 3.1 1.5 1.0
C1D I:HEM304 3.1 1.5 1.0
C1B I:HEM304 3.1 1.5 1.0
C4A I:HEM304 3.1 1.5 1.0
C1A I:HEM304 3.1 1.5 1.0
CE1 I:HIS107 3.3 1.8 1.0
CD2 I:HIS209 3.3 1.7 1.0
CHC I:HEM304 3.4 1.5 1.0
CHD I:HEM304 3.4 1.5 1.0
CHA I:HEM304 3.4 1.5 1.0
CHB I:HEM304 3.4 1.5 1.0
ND1 I:HIS209 4.0 1.7 1.0
CG I:HIS107 4.0 1.8 1.0
ND1 I:HIS107 4.2 1.8 1.0
C2C I:HEM304 4.2 1.5 1.0
C3C I:HEM304 4.2 1.5 1.0
C3D I:HEM304 4.2 1.5 1.0
C2D I:HEM304 4.3 1.5 1.0
C2B I:HEM304 4.3 1.5 1.0
C3B I:HEM304 4.3 1.5 1.0
C3A I:HEM304 4.3 1.5 1.0
CG I:HIS209 4.3 1.7 1.0
C2A I:HEM304 4.3 1.5 1.0

Iron binding site 9 out of 12 in 7zxy

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Iron binding site 9 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe305

b:4.1
occ:1.00
FE I:HEC305 0.0 4.1 1.0
NC I:HEC305 2.0 4.1 1.0
NA I:HEC305 2.0 4.1 1.0
ND I:HEC305 2.0 4.1 1.0
NB I:HEC305 2.0 4.1 1.0
C1B I:HEC305 3.0 4.1 1.0
C4C I:HEC305 3.0 4.1 1.0
C4B I:HEC305 3.0 4.1 1.0
C4A I:HEC305 3.1 4.1 1.0
C1D I:HEC305 3.1 4.1 1.0
C4D I:HEC305 3.1 4.1 1.0
C1C I:HEC305 3.1 4.1 1.0
C1A I:HEC305 3.1 4.1 1.0
CZ J:PHE40 3.2 8.1 1.0
CHB I:HEC305 3.4 4.1 1.0
CHD I:HEC305 3.4 4.1 1.0
CHC I:HEC305 3.4 4.1 1.0
CHA I:HEC305 3.4 4.1 1.0
CE2 J:PHE40 3.7 8.1 1.0
CE1 J:PHE40 3.8 8.1 1.0
O2A I:HEM304 4.0 1.5 1.0
C2B I:HEC305 4.2 4.1 1.0
C3B I:HEC305 4.2 4.1 1.0
C3C I:HEC305 4.3 4.1 1.0
C3A I:HEC305 4.3 4.1 1.0
C3D I:HEC305 4.3 4.1 1.0
C2D I:HEC305 4.3 4.1 1.0
C2C I:HEC305 4.3 4.1 1.0
C2A I:HEC305 4.3 4.1 1.0
O I:TYR41 4.4 5.3 1.0
CMA I:HEM304 4.5 1.5 1.0
CD2 J:PHE40 4.6 8.1 1.0
CA I:GLY45 4.7 4.0 1.0
CD1 J:PHE40 4.7 8.1 1.0
N I:GLY45 4.9 4.0 1.0
CGA I:HEM304 4.9 1.5 1.0

Iron binding site 10 out of 12 in 7zxy

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Iron binding site 10 out of 12 in the 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of 3.15 Angstrom Cryo-Em Structure of the Dimeric Cytochrome B6F Complex From Synechocystis Sp. Pcc 6803 with Natively Bound Plastoquinone and Lipid Molecules. within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Fe301

b:23.3
occ:1.00
FE K:HEC301 0.0 23.3 1.0
NC K:HEC301 2.0 23.3 1.0
NE2 K:HIS26 2.0 20.8 1.0
NA K:HEC301 2.0 23.3 1.0
NB K:HEC301 2.1 23.3 1.0
ND K:HEC301 2.1 23.3 1.0
N K:TYR1 2.6 23.8 1.0
CE1 K:HIS26 2.7 20.8 1.0
C4C K:HEC301 3.0 23.3 1.0
C4A K:HEC301 3.1 23.3 1.0
C1D K:HEC301 3.1 23.3 1.0
C1B K:HEC301 3.1 23.3 1.0
C1A K:HEC301 3.1 23.3 1.0
C1C K:HEC301 3.1 23.3 1.0
C4B K:HEC301 3.1 23.3 1.0
C4D K:HEC301 3.1 23.3 1.0
CD2 K:HIS26 3.3 20.8 1.0
CHD K:HEC301 3.4 23.3 1.0
CHB K:HEC301 3.4 23.3 1.0
CHA K:HEC301 3.4 23.3 1.0
CHC K:HEC301 3.5 23.3 1.0
CA K:TYR1 3.6 23.8 1.0
ND1 K:HIS26 3.9 20.8 1.0
C K:TYR1 4.2 23.8 1.0
CG K:HIS26 4.2 20.8 1.0
C3C K:HEC301 4.3 23.3 1.0
C3A K:HEC301 4.3 23.3 1.0
C2C K:HEC301 4.3 23.3 1.0
C2A K:HEC301 4.3 23.3 1.0
C2B K:HEC301 4.3 23.3 1.0
C3B K:HEC301 4.3 23.3 1.0
C2D K:HEC301 4.3 23.3 1.0
C3D K:HEC301 4.3 23.3 1.0
O K:TYR1 4.3 23.8 1.0
ND2 K:ASN154 4.6 16.3 1.0
CB K:TYR1 4.9 23.8 1.0
N K:GLY158 5.0 25.6 1.0
CA K:GLY158 5.0 25.6 1.0

Reference:

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
Page generated: Fri Aug 9 15:43:56 2024

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