Iron in PDB 7deg: Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism

Other elements in 7deg:

The structure of Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism also contains other interesting chemical elements:

Copper (Cu) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism (pdb code 7deg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism, PDB code: 7deg:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7deg

Go back to Iron Binding Sites List in 7deg
Iron binding site 1 out of 4 in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism


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 A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:24.4
occ:1.00
FE A:HAS601 0.0 24.4 1.0
NE2 A:HIS383 1.9 19.1 1.0
ND A:HAS601 2.1 24.4 1.0
NC A:HAS601 2.1 24.4 1.0
NA A:HAS601 2.1 24.4 1.0
NB A:HAS601 2.1 24.4 1.0
CD2 A:HIS383 2.8 19.1 1.0
CE1 A:HIS383 2.9 19.1 1.0
C1A A:HAS601 3.0 24.4 1.0
C1C A:HAS601 3.1 24.4 1.0
C4D A:HAS601 3.1 24.4 1.0
C1D A:HAS601 3.1 24.4 1.0
C4C A:HAS601 3.1 24.4 1.0
C1B A:HAS601 3.1 24.4 1.0
C4A A:HAS601 3.1 24.4 1.0
C4B A:HAS601 3.1 24.4 1.0
CHC A:HAS601 3.6 24.4 1.0
CHA A:HAS601 3.6 24.4 1.0
CHB A:HAS601 3.6 24.4 1.0
CHD A:HAS601 3.6 24.4 1.0
CE1 A:HIS222 3.9 30.1 1.0
CG A:HIS383 4.0 19.1 1.0
ND1 A:HIS383 4.0 19.1 1.0
C3C A:HAS601 4.3 24.4 1.0
C2D A:HAS601 4.3 24.4 1.0
C2C A:HAS601 4.3 24.4 1.0
C2A A:HAS601 4.3 24.4 1.0
C2B A:HAS601 4.3 24.4 1.0
C3D A:HAS601 4.3 24.4 1.0
C3A A:HAS601 4.3 24.4 1.0
C3B A:HAS601 4.3 24.4 1.0
CG1 A:VAL225 4.5 23.9 1.0
NE2 A:HIS222 4.6 30.1 1.0
ND1 A:HIS222 4.8 30.1 1.0
CG2 A:VAL225 4.9 23.9 1.0

Iron binding site 2 out of 4 in 7deg

Go back to Iron Binding Sites List in 7deg
Iron binding site 2 out of 4 in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism


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 A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:17.6
occ:1.00
FE A:HEM602 0.0 17.6 1.0
NE2 A:HIS60 1.7 16.8 1.0
NC A:HEM602 1.9 17.6 1.0
NA A:HEM602 2.0 17.6 1.0
CE1 A:HIS60 2.0 16.8 1.0
NB A:HEM602 2.0 17.6 1.0
ND A:HEM602 2.0 17.6 1.0
NE2 A:HIS385 2.5 17.2 1.0
C1C A:HEM602 3.0 17.6 1.0
C4C A:HEM602 3.0 17.6 1.0
C4A A:HEM602 3.0 17.6 1.0
C1A A:HEM602 3.0 17.6 1.0
C1B A:HEM602 3.0 17.6 1.0
CD2 A:HIS60 3.0 16.8 1.0
C4D A:HEM602 3.0 17.6 1.0
C1D A:HEM602 3.0 17.6 1.0
C4B A:HEM602 3.1 17.6 1.0
CE1 A:HIS385 3.2 17.2 1.0
ND1 A:HIS60 3.3 16.8 1.0
CHB A:HEM602 3.4 17.6 1.0
CHA A:HEM602 3.4 17.6 1.0
CHC A:HEM602 3.4 17.6 1.0
CHD A:HEM602 3.4 17.6 1.0
CD2 A:HIS385 3.5 17.2 1.0
CG A:HIS60 3.8 16.8 1.0
C2C A:HEM602 4.2 17.6 1.0
C3C A:HEM602 4.2 17.6 1.0
C2A A:HEM602 4.2 17.6 1.0
C3A A:HEM602 4.2 17.6 1.0
C3D A:HEM602 4.2 17.6 1.0
C2B A:HEM602 4.2 17.6 1.0
C2D A:HEM602 4.2 17.6 1.0
C3B A:HEM602 4.3 17.6 1.0
ND1 A:HIS385 4.4 17.2 1.0
CG A:HIS385 4.5 17.2 1.0
CA A:GLY32 4.8 17.9 1.0

Iron binding site 3 out of 4 in 7deg

Go back to Iron Binding Sites List in 7deg
Iron binding site 3 out of 4 in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism


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 A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe602

b:24.4
occ:1.00
FE D:HAS602 0.0 24.4 1.0
NE2 D:HIS383 1.9 19.1 1.0
ND D:HAS602 2.1 24.4 1.0
NC D:HAS602 2.1 24.4 1.0
NA D:HAS602 2.1 24.4 1.0
NB D:HAS602 2.1 24.4 1.0
CD2 D:HIS383 2.8 19.1 1.0
CE1 D:HIS383 2.9 19.1 1.0
C1A D:HAS602 3.0 24.4 1.0
C1C D:HAS602 3.1 24.4 1.0
C4D D:HAS602 3.1 24.4 1.0
C1D D:HAS602 3.1 24.4 1.0
C4C D:HAS602 3.1 24.4 1.0
C1B D:HAS602 3.1 24.4 1.0
C4A D:HAS602 3.1 24.4 1.0
C4B D:HAS602 3.1 24.4 1.0
CHC D:HAS602 3.6 24.4 1.0
CHA D:HAS602 3.6 24.4 1.0
CHB D:HAS602 3.6 24.4 1.0
CHD D:HAS602 3.6 24.4 1.0
CE1 D:HIS222 3.9 30.1 1.0
CG D:HIS383 4.0 19.1 1.0
ND1 D:HIS383 4.0 19.1 1.0
C3C D:HAS602 4.3 24.4 1.0
C2D D:HAS602 4.3 24.4 1.0
C2C D:HAS602 4.3 24.4 1.0
C2A D:HAS602 4.3 24.4 1.0
C2B D:HAS602 4.3 24.4 1.0
C3D D:HAS602 4.3 24.4 1.0
C3A D:HAS602 4.3 24.4 1.0
C3B D:HAS602 4.3 24.4 1.0
CG1 D:VAL225 4.5 23.9 1.0
NE2 D:HIS222 4.6 30.1 1.0
ND1 D:HIS222 4.8 30.1 1.0
CG2 D:VAL225 4.9 23.9 1.0

Iron binding site 4 out of 4 in 7deg

Go back to Iron Binding Sites List in 7deg
Iron binding site 4 out of 4 in the Cryo-Em Structure of A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism


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 A Heme-Copper Terminal Oxidase Dimer Provides Insights Into Its Catalytic Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe603

b:17.6
occ:1.00
FE D:HEM603 0.0 17.6 1.0
NE2 D:HIS60 1.7 16.8 1.0
NC D:HEM603 1.9 17.6 1.0
NA D:HEM603 2.0 17.6 1.0
CE1 D:HIS60 2.0 16.8 1.0
NB D:HEM603 2.0 17.6 1.0
ND D:HEM603 2.0 17.6 1.0
NE2 D:HIS385 2.4 17.2 1.0
C1C D:HEM603 3.0 17.6 1.0
C4C D:HEM603 3.0 17.6 1.0
C4A D:HEM603 3.0 17.6 1.0
C1A D:HEM603 3.0 17.6 1.0
C1B D:HEM603 3.0 17.6 1.0
CD2 D:HIS60 3.0 16.8 1.0
C4D D:HEM603 3.0 17.6 1.0
C1D D:HEM603 3.0 17.6 1.0
C4B D:HEM603 3.1 17.6 1.0
CE1 D:HIS385 3.2 17.2 1.0
ND1 D:HIS60 3.3 16.8 1.0
CHB D:HEM603 3.4 17.6 1.0
CHA D:HEM603 3.4 17.6 1.0
CHC D:HEM603 3.4 17.6 1.0
CHD D:HEM603 3.4 17.6 1.0
CD2 D:HIS385 3.5 17.2 1.0
CG D:HIS60 3.8 16.8 1.0
C2C D:HEM603 4.2 17.6 1.0
C3C D:HEM603 4.2 17.6 1.0
C2A D:HEM603 4.2 17.6 1.0
C3A D:HEM603 4.2 17.6 1.0
C3D D:HEM603 4.2 17.6 1.0
C2B D:HEM603 4.2 17.6 1.0
C2D D:HEM603 4.2 17.6 1.0
C3B D:HEM603 4.3 17.6 1.0
ND1 D:HIS385 4.4 17.2 1.0
CG D:HIS385 4.5 17.2 1.0
CA D:GLY32 4.8 17.9 1.0

Reference:

G.Zhu, H.Zeng, S.Zhang, J.Juli, L.Tai, D.Zhang, X.Pang, Y.Zhang, S.M.Lam, Y.Zhu, G.Peng, H.Michel, F.Sun. The Unusual Homodimer of A Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors. Angew.Chem.Int.Ed.Engl. V. 60 13323 2021.
ISSN: ESSN 1521-3773
PubMed: 33665933
DOI: 10.1002/ANIE.202016785
Page generated: Sat Aug 21 14:14:09 2021

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