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Iron in PDB 9iig: Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Enzymatic activity of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
All present enzymatic activity of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis:
1.16.3.1;
1.16.3.1;
Other elements in 9iig:
The structure of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis also contains other interesting chemical elements:
| Sodium | (Na) | 6 atoms |
Iron Binding Sites:
The binding sites of Iron atom in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
(pdb code 9iig). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis, PDB code: 9iig:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;
In total 6 binding sites of Iron where determined in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis, PDB code: 9iig:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;
Iron binding site 1 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 1 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
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 Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Iron binding site 2 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 2 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
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 Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Iron binding site 3 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 3 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Iron binding site 4 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 4 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Iron binding site 5 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 5 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Iron binding site 6 out of 6 in 9iig
Go back to
Iron Binding Sites List in 9iig
Iron binding site 6 out
of 6 in the Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Cryo-Em Structure of Hetero-Bacterioferritin SOBFR12 From Shewanella Oneidensis within 5.0Å range:
|
Reference:
Y.Li,
W.Wang,
W.Wang,
X.Zhang,
J.Chen,
H.Gao.
Unveiling Structural Heterogeneity and Evolutionary Adaptations of Heteromultimeric Bacterioferritin Nanocages. Adv Sci 09957 2025.
ISSN: ESSN 2198-3844
PubMed: 40167232
DOI: 10.1002/ADVS.202409957
Page generated: Fri Aug 8 06:48:49 2025
ISSN: ESSN 2198-3844
PubMed: 40167232
DOI: 10.1002/ADVS.202409957
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