Iron in PDB 8qqk: Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs

Enzymatic activity of Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs

All present enzymatic activity of Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs:
7.1.1.3;

Other elements in 8qqk:

The structure of Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs also contains other interesting chemical elements:

Copper (Cu) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs (pdb code 8qqk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs, PDB code: 8qqk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 8qqk

Go back to Iron Binding Sites List in 8qqk
Iron binding site 1 out of 2 in the Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe705

b:49.1
occ:1.00
FE A:HEM705 0.0 49.1 1.0
ND A:HEM705 1.9 49.1 1.0
NA A:HEM705 2.0 49.1 1.0
NC A:HEM705 2.1 49.1 1.0
NB A:HEM705 2.1 49.1 1.0
NE2 A:HIS421 2.4 48.7 1.0
C4D A:HEM705 2.8 49.1 1.0
C1D A:HEM705 2.9 49.1 1.0
NE2 A:HIS106 2.9 49.8 1.0
C1A A:HEM705 2.9 49.1 1.0
C4A A:HEM705 3.0 49.1 1.0
C4C A:HEM705 3.1 49.1 1.0
C4B A:HEM705 3.1 49.1 1.0
C1B A:HEM705 3.1 49.1 1.0
C1C A:HEM705 3.1 49.1 1.0
CD2 A:HIS421 3.3 48.7 1.0
CHA A:HEM705 3.3 49.1 1.0
CE1 A:HIS421 3.3 48.7 1.0
CHD A:HEM705 3.4 49.1 1.0
CHB A:HEM705 3.5 49.1 1.0
CHC A:HEM705 3.5 49.1 1.0
CD2 A:HIS106 3.7 49.8 1.0
CE1 A:HIS106 3.9 49.8 1.0
C3D A:HEM705 4.1 49.1 1.0
C2D A:HEM705 4.1 49.1 1.0
C2A A:HEM705 4.2 49.1 1.0
C3A A:HEM705 4.2 49.1 1.0
C3C A:HEM705 4.3 49.1 1.0
C2C A:HEM705 4.3 49.1 1.0
C2B A:HEM705 4.3 49.1 1.0
C3B A:HEM705 4.3 49.1 1.0
CG A:HIS421 4.4 48.7 1.0
ND1 A:HIS421 4.4 48.7 1.0
CG A:MET110 4.8 49.6 1.0
CG A:HIS106 4.9 49.8 1.0
CE1 A:PHE420 4.9 49.0 1.0
ND1 A:HIS106 5.0 49.8 1.0

Iron binding site 2 out of 2 in 8qqk

Go back to Iron Binding Sites List in 8qqk
Iron binding site 2 out of 2 in the Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of E. Coli Cytochrome BO3 Quinol Oxidase Assembled in Peptidiscs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe706

b:51.3
occ:1.00
FE A:HEO706 0.0 51.3 1.0
NC A:HEO706 2.0 51.3 1.0
NA A:HEO706 2.0 51.3 1.0
ND A:HEO706 2.0 51.3 1.0
NB A:HEO706 2.0 51.3 1.0
NE2 A:HIS419 2.4 48.7 1.0
C1C A:HEO706 3.0 51.3 1.0
C1A A:HEO706 3.1 51.3 1.0
C4D A:HEO706 3.1 51.3 1.0
C4B A:HEO706 3.1 51.3 1.0
C4C A:HEO706 3.1 51.3 1.0
C1B A:HEO706 3.1 51.3 1.0
C4A A:HEO706 3.1 51.3 1.0
C1D A:HEO706 3.1 51.3 1.0
CD2 A:HIS419 3.1 48.7 1.0
CHC A:HEO706 3.5 51.3 1.0
CHA A:HEO706 3.5 51.3 1.0
CE1 A:HIS419 3.6 48.7 1.0
CHB A:HEO706 3.6 51.3 1.0
CHD A:HEO706 3.6 51.3 1.0
C3C A:HEO706 4.3 51.3 1.0
C2C A:HEO706 4.3 51.3 1.0
C2A A:HEO706 4.3 51.3 1.0
C2B A:HEO706 4.3 51.3 1.0
C3B A:HEO706 4.3 51.3 1.0
C3D A:HEO706 4.3 51.3 1.0
C3A A:HEO706 4.3 51.3 1.0
C2D A:HEO706 4.3 51.3 1.0
CG A:HIS419 4.4 48.7 1.0
CU A:CU707 4.4 60.4 1.0
CE1 A:HIS284 4.6 49.8 1.0
ND1 A:HIS419 4.6 48.7 1.0
CG2 A:VAL423 4.6 49.9 1.0

Reference:

Y.Gao, Y.Zhang, S.Hakke, R.Mohren, L.J.P.M.Sijbers, P.J.Peters, R.B.G.Ravelli. Cryo-Em Structure of Cytochrome Bo 3 Quinol Oxidase Assembled in Peptidiscs Reveals An "Open" Conformation For Potential Ubiquinone-8 Release. Biochim Biophys Acta 49045 2024BIOENERG.
ISSN: ISSN 1879-2650
PubMed: 38614453
DOI: 10.1016/J.BBABIO.2024.149045
Page generated: Sat Aug 10 15:43:53 2024

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