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Iron in PDB 8f6c: E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer

Enzymatic activity of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer

All present enzymatic activity of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer:
7.1.1.3;

Other elements in 8f6c:

The structure of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer (pdb code 8f6c). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer, PDB code: 8f6c:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8f6c

Go back to Iron Binding Sites List in 8f6c
Iron binding site 1 out of 4 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1001

b:28.5
occ:1.00
FE A:HEM1001 0.0 28.5 1.0
ND A:HEM1001 1.9 28.6 1.0
NA A:HEM1001 2.0 28.6 1.0
NE2 A:HIS421 2.0 28.8 1.0
NC A:HEM1001 2.1 28.5 1.0
NB A:HEM1001 2.1 28.5 1.0
NE2 A:HIS106 2.6 29.0 1.0
CE1 A:HIS421 2.6 28.8 1.0
C4D A:HEM1001 2.9 28.6 1.0
C1D A:HEM1001 2.9 28.6 1.0
C1A A:HEM1001 3.0 28.6 1.0
C4C A:HEM1001 3.0 28.5 1.0
C4A A:HEM1001 3.0 28.6 1.0
C1B A:HEM1001 3.1 28.6 1.0
C4B A:HEM1001 3.1 28.6 1.0
C1C A:HEM1001 3.1 28.5 1.0
CD2 A:HIS421 3.2 28.8 1.0
CD2 A:HIS106 3.3 29.0 1.0
CHA A:HEM1001 3.3 28.6 1.0
CHD A:HEM1001 3.4 28.5 1.0
CHB A:HEM1001 3.5 28.6 1.0
CHC A:HEM1001 3.5 28.5 1.0
CE1 A:HIS106 3.7 29.0 1.0
ND1 A:HIS421 3.9 28.8 1.0
C3D A:HEM1001 4.1 28.6 1.0
C2D A:HEM1001 4.2 28.6 1.0
CG A:HIS421 4.2 28.8 1.0
C2A A:HEM1001 4.2 28.6 1.0
C3A A:HEM1001 4.2 28.6 1.0
C3C A:HEM1001 4.3 28.5 1.0
C2C A:HEM1001 4.3 28.5 1.0
C2B A:HEM1001 4.3 28.6 1.0
C3B A:HEM1001 4.4 28.6 1.0
CG A:HIS106 4.5 29.0 1.0
ND1 A:HIS106 4.7 29.0 1.0
CE1 A:PHE420 4.7 28.9 1.0
CZ A:PHE420 4.9 28.9 1.0

Iron binding site 2 out of 4 in 8f6c

Go back to Iron Binding Sites List in 8f6c
Iron binding site 2 out of 4 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1002

b:29.5
occ:1.00
FE A:HEO1002 0.0 29.5 1.0
NA A:HEO1002 2.0 29.5 1.0
NC A:HEO1002 2.0 29.5 1.0
NB A:HEO1002 2.0 29.5 1.0
ND A:HEO1002 2.0 29.5 1.0
NE2 A:HIS419 2.0 28.9 1.0
CD2 A:HIS419 2.7 28.9 1.0
C4C A:HEO1002 3.0 29.5 1.0
C4A A:HEO1002 3.0 29.5 1.0
C1D A:HEO1002 3.0 29.5 1.0
C1B A:HEO1002 3.1 29.5 1.0
C1C A:HEO1002 3.2 29.5 1.0
C1A A:HEO1002 3.2 29.5 1.0
C4B A:HEO1002 3.2 29.5 1.0
C4D A:HEO1002 3.2 29.5 1.0
CE1 A:HIS419 3.3 28.9 1.0
CHD A:HEO1002 3.4 29.5 1.0
CHB A:HEO1002 3.4 29.5 1.0
CHC A:HEO1002 3.7 29.5 1.0
CHA A:HEO1002 3.7 29.5 1.0
CG A:HIS419 3.9 28.9 1.0
ND1 A:HIS419 4.2 28.9 1.0
CG2 A:VAL423 4.2 29.0 1.0
C3C A:HEO1002 4.3 29.5 1.0
C3A A:HEO1002 4.4 29.5 1.0
C2B A:HEO1002 4.4 29.6 1.0
C2D A:HEO1002 4.4 29.5 1.0
C2C A:HEO1002 4.4 29.5 1.0
C2A A:HEO1002 4.4 29.5 1.0
C3B A:HEO1002 4.4 29.6 1.0
C3D A:HEO1002 4.5 29.5 1.0
CA A:PHE420 4.8 28.9 1.0
CB A:PHE420 4.9 28.9 1.0

Iron binding site 3 out of 4 in 8f6c

Go back to Iron Binding Sites List in 8f6c
Iron binding site 3 out of 4 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1001

b:28.5
occ:1.00
FE E:HEM1001 0.0 28.5 1.0
ND E:HEM1001 1.9 28.6 1.0
NA E:HEM1001 2.0 28.6 1.0
NE2 E:HIS421 2.0 28.8 1.0
NC E:HEM1001 2.1 28.6 1.0
NB E:HEM1001 2.1 28.6 1.0
NE2 E:HIS106 2.6 29.0 1.0
CE1 E:HIS421 2.6 28.8 1.0
C4D E:HEM1001 2.9 28.6 1.0
C1D E:HEM1001 2.9 28.6 1.0
C1A E:HEM1001 3.0 28.6 1.0
C4C E:HEM1001 3.0 28.5 1.0
C4A E:HEM1001 3.0 28.6 1.0
C1B E:HEM1001 3.1 28.6 1.0
C4B E:HEM1001 3.1 28.6 1.0
C1C E:HEM1001 3.1 28.6 1.0
CD2 E:HIS421 3.2 28.8 1.0
CD2 E:HIS106 3.3 29.0 1.0
CHA E:HEM1001 3.3 28.6 1.0
CHD E:HEM1001 3.4 28.6 1.0
CHB E:HEM1001 3.5 28.6 1.0
CHC E:HEM1001 3.5 28.6 1.0
CE1 E:HIS106 3.7 29.0 1.0
ND1 E:HIS421 3.9 28.8 1.0
C3D E:HEM1001 4.1 28.6 1.0
C2D E:HEM1001 4.2 28.6 1.0
CG E:HIS421 4.2 28.8 1.0
C2A E:HEM1001 4.2 28.6 1.0
C3A E:HEM1001 4.2 28.6 1.0
C3C E:HEM1001 4.3 28.5 1.0
C2C E:HEM1001 4.3 28.5 1.0
C2B E:HEM1001 4.3 28.6 1.0
C3B E:HEM1001 4.4 28.6 1.0
CG E:HIS106 4.5 29.0 1.0
ND1 E:HIS106 4.7 29.0 1.0
CE1 E:PHE420 4.7 28.9 1.0
CZ E:PHE420 4.9 28.9 1.0

Iron binding site 4 out of 4 in 8f6c

Go back to Iron Binding Sites List in 8f6c
Iron binding site 4 out of 4 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1002

b:29.5
occ:1.00
FE E:HEO1002 0.0 29.5 1.0
NA E:HEO1002 2.0 29.5 1.0
NC E:HEO1002 2.0 29.5 1.0
NB E:HEO1002 2.0 29.5 1.0
ND E:HEO1002 2.0 29.5 1.0
NE2 E:HIS419 2.0 28.9 1.0
CD2 E:HIS419 2.7 28.9 1.0
C4C E:HEO1002 3.0 29.5 1.0
C4A E:HEO1002 3.0 29.5 1.0
C1D E:HEO1002 3.0 29.5 1.0
C1B E:HEO1002 3.1 29.5 1.0
C1C E:HEO1002 3.2 29.5 1.0
C1A E:HEO1002 3.2 29.5 1.0
C4B E:HEO1002 3.2 29.5 1.0
C4D E:HEO1002 3.2 29.5 1.0
CE1 E:HIS419 3.3 28.9 1.0
CHD E:HEO1002 3.4 29.5 1.0
CHB E:HEO1002 3.4 29.5 1.0
CHC E:HEO1002 3.7 29.5 1.0
CHA E:HEO1002 3.7 29.5 1.0
CG E:HIS419 3.9 28.9 1.0
ND1 E:HIS419 4.2 28.9 1.0
CG2 E:VAL423 4.2 29.0 1.0
C3C E:HEO1002 4.3 29.5 1.0
C3A E:HEO1002 4.4 29.5 1.0
C2B E:HEO1002 4.4 29.6 1.0
C2D E:HEO1002 4.4 29.5 1.0
C2C E:HEO1002 4.4 29.5 1.0
C2A E:HEO1002 4.4 29.5 1.0
C3B E:HEO1002 4.4 29.6 1.0
C3D E:HEO1002 4.5 29.5 1.0
CA E:PHE420 4.8 28.9 1.0
CB E:PHE420 4.9 28.9 1.0

Reference:

Y.Guo, E.Karimullina, D.Borek, A.Savchenko. Monomer and Dimer Structures of E. Coli Cytochrome BO3 Ubiquinol Oxidase To Be Published.
Page generated: Sat Aug 10 02:40:00 2024

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