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Iron in PDB 7jz2: Succinate: Quinone Oxidoreductase Sqr From E.Coli K12

Enzymatic activity of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12

All present enzymatic activity of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12:
1.3.5.1;

Other elements in 7jz2:

The structure of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Iron atom in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 (pdb code 7jz2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12, PDB code: 7jz2:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in 7jz2

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Iron binding site 1 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:28.0
occ:1.00
 FE1 B:FES301 0.0 28.0 1.0
S1 B:FES301 2.2 28.0 1.0
S2 B:FES301 2.2 28.0 1.0
OD1 B:ASP63 2.6 24.5 1.0
SG B:CYS75 2.9 25.5 1.0
FE2 B:FES301 3.1 28.0 1.0
CG B:ASP63 3.3 24.5 1.0
OD2 B:ASP63 3.6 24.5 1.0
CA B:GLY58 3.6 27.5 1.0
SG B:CYS55 3.7 26.4 1.0
CB B:CYS75 3.8 25.5 1.0
N B:GLY58 3.8 27.5 1.0
CB B:LEU73 4.3 22.9 1.0
N B:ASP63 4.3 24.5 1.0
CD1 B:LEU73 4.4 22.9 1.0
N B:SER62 4.5 23.2 1.0
CD2 B:LEU73 4.5 22.9 1.0
CB B:ASP63 4.6 24.5 1.0
CG B:LEU73 4.6 22.9 1.0
N B:CYS75 4.7 25.5 1.0
C B:GLY58 4.7 27.5 1.0
N B:GLY61 4.8 22.6 1.0
N B:ARG56 4.8 28.0 1.0
CA B:CYS75 4.8 25.5 1.0
C B:GLU57 4.9 28.4 1.0
CA B:ASP63 4.9 24.5 1.0
N B:VAL59 5.0 24.9 1.0

Iron binding site 2 out of 30 in 7jz2

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Iron binding site 2 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:28.0
occ:1.00
 FE2 B:FES301 0.0 28.0 1.0
S2 B:FES301 2.2 28.0 1.0
S1 B:FES301 2.2 28.0 1.0
SG B:CYS55 3.0 26.4 1.0
FE1 B:FES301 3.1 28.0 1.0
N B:CYS55 3.1 26.4 1.0
SG B:CYS60 3.1 22.3 1.0
CB B:SER62 3.2 23.2 1.0
N B:SER54 3.2 24.3 1.0
OG B:SER62 3.7 23.2 1.0
N B:SER62 3.7 23.2 1.0
N B:ARG56 3.9 28.0 1.0
CA B:SER62 3.9 23.2 1.0
CA B:SER54 3.9 24.3 1.0
C B:SER54 3.9 24.3 1.0
N B:ASP63 4.0 24.5 1.0
CB B:CYS55 4.0 26.4 1.0
CA B:CYS55 4.0 26.4 1.0
C B:ARG53 4.2 25.5 1.0
OD1 B:ASP63 4.2 24.5 1.0
CB B:SER54 4.2 24.3 1.0
CA B:ARG53 4.2 25.5 1.0
CG B:ASP63 4.4 24.5 1.0
C B:SER62 4.5 23.2 1.0
C B:CYS55 4.5 26.4 1.0
N B:GLY61 4.6 22.6 1.0
OD2 B:ASP63 4.8 24.5 1.0
C B:GLY61 4.8 22.6 1.0
CB B:CYS60 4.8 22.3 1.0
CB B:ASP63 4.9 24.5 1.0
CA B:ARG56 4.9 28.0 1.0

Iron binding site 3 out of 30 in 7jz2

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Iron binding site 3 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:28.0
occ:1.00
 FE1 B:SF4302 0.0 28.0 1.0
S4 B:SF4302 2.3 28.0 1.0
S3 B:SF4302 2.3 28.0 1.0
S2 B:SF4302 2.3 28.0 1.0
FE2 B:SF4302 2.7 28.0 1.0
FE4 B:SF4302 2.7 28.0 1.0
FE3 B:SF4302 2.7 28.0 1.0
SG B:CYS155 2.9 22.5 1.0
CB B:CYS155 3.1 22.5 1.0
S1 B:SF4302 3.9 28.0 1.0
CA B:CYS155 4.3 22.5 1.0
N B:CYS155 4.4 22.5 1.0
CB B:ALA173 4.4 23.1 1.0
SG B:CYS216 4.7 23.1 1.0
CG B:PRO222 4.7 24.3 1.0
CA B:ALA173 4.8 23.1 1.0
SG B:CYS149 4.9 26.1 1.0

Iron binding site 4 out of 30 in 7jz2

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Iron binding site 4 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:28.0
occ:1.00
 FE2 B:SF4302 0.0 28.0 1.0
S4 B:SF4302 2.3 28.0 1.0
S3 B:SF4302 2.3 28.0 1.0
S1 B:SF4302 2.3 28.0 1.0
FE1 B:SF4302 2.7 28.0 1.0
FE3 B:SF4302 2.7 28.0 1.0
FE4 B:SF4302 2.7 28.0 1.0
SG B:CYS216 3.0 23.1 1.0
CD B:PRO217 3.4 22.1 1.0
S2 B:SF4302 3.9 28.0 1.0
N B:PRO217 4.1 22.1 1.0
CA B:CYS216 4.1 23.1 1.0
CB B:CYS216 4.1 23.1 1.0
N B:LYS218 4.3 23.5 1.0
C B:CYS216 4.5 23.1 1.0
CB B:LYS218 4.5 23.5 1.0
CG B:PRO217 4.5 22.1 1.0
CD1 B:LEU220 4.7 23.1 1.0
CG B:LYS218 4.7 23.5 1.0
SG B:CYS152 4.8 23.0 1.0
CB B:LEU220 4.8 23.1 1.0
CG B:LEU220 4.9 23.1 1.0
CA B:LYS218 4.9 23.5 1.0

Iron binding site 5 out of 30 in 7jz2

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Iron binding site 5 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:28.0
occ:1.00
 FE3 B:SF4302 0.0 28.0 1.0
S1 B:SF4302 2.3 28.0 1.0
S4 B:SF4302 2.3 28.0 1.0
S2 B:SF4302 2.3 28.0 1.0
FE2 B:SF4302 2.7 28.0 1.0
FE4 B:SF4302 2.7 28.0 1.0
FE1 B:SF4302 2.7 28.0 1.0
SG B:CYS149 2.9 26.1 1.0
CA B:CYS149 3.5 26.1 1.0
CB B:CYS149 3.6 26.1 1.0
S3 B:SF4302 3.9 28.0 1.0
N B:ILE150 4.0 23.2 1.0
C B:CYS149 4.2 26.1 1.0
N B:LEU151 4.3 22.9 1.0
CD1 B:LEU220 4.4 23.1 1.0
N B:CYS149 4.7 26.1 1.0
CB B:ALA173 5.0 23.1 1.0
CA B:LEU151 5.0 22.9 1.0
CG1 B:ILE150 5.0 23.2 1.0

Iron binding site 6 out of 30 in 7jz2

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Iron binding site 6 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:28.0
occ:1.00
 FE4 B:SF4302 0.0 28.0 1.0
S2 B:SF4302 2.3 28.0 1.0
S1 B:SF4302 2.3 28.0 1.0
S3 B:SF4302 2.3 28.0 1.0
FE1 B:SF4302 2.7 28.0 1.0
FE3 B:SF4302 2.7 28.0 1.0
FE2 B:SF4302 2.7 28.0 1.0
SG B:CYS152 2.9 23.0 1.0
S4 B:SF4302 3.9 28.0 1.0
N B:CYS152 3.9 23.0 1.0
N B:ALA153 4.1 21.7 1.0
N B:CYS154 4.1 20.4 1.0
CB B:CYS152 4.3 23.0 1.0
CD B:PRO217 4.3 22.1 1.0
SG B:CYS155 4.4 22.5 1.0
N B:CYS155 4.4 22.5 1.0
CA B:CYS152 4.4 23.0 1.0
C B:CYS152 4.5 23.0 1.0
CB B:CYS154 4.7 20.4 1.0
CB B:CYS155 4.7 22.5 1.0
N B:LEU151 4.7 22.9 1.0
CG1 B:ILE150 4.8 23.2 1.0
CA B:CYS154 4.8 20.4 1.0
C B:ALA153 4.9 21.7 1.0
CA B:ALA153 4.9 21.7 1.0
CG B:PRO217 4.9 22.1 1.0
SG B:CYS149 4.9 26.1 1.0
CA B:LEU151 4.9 22.9 1.0
C B:LEU151 4.9 22.9 1.0

Iron binding site 7 out of 30 in 7jz2

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Iron binding site 7 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:34.1
occ:1.00
 FE1 B:F3S303 0.0 34.1 1.0
S1 B:F3S303 2.2 34.1 1.0
S2 B:F3S303 2.3 34.1 1.0
S3 B:F3S303 2.3 34.1 1.0
FE4 B:F3S303 2.7 34.1 1.0
FE3 B:F3S303 2.7 34.1 1.0
SG B:CYS159 2.9 23.9 1.0
CB B:CYS159 3.8 23.9 1.0
S4 B:F3S303 3.9 34.1 1.0
CB B:ILE209 4.2 26.6 1.0
SG B:CYS206 4.3 25.9 1.0
CD1 B:ILE209 4.3 26.6 1.0
CG1 B:ILE209 4.4 26.6 1.0
N B:ILE209 4.6 26.6 1.0
CA B:CYS159 4.8 23.9 1.0
N B:MET210 4.8 27.7 1.0
CB B:CYS206 4.9 25.9 1.0
OG B:SER161 5.0 23.3 1.0
CA B:ILE209 5.0 26.6 1.0
CA B:CYS206 5.0 25.9 1.0

Iron binding site 8 out of 30 in 7jz2

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Iron binding site 8 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:34.1
occ:1.00
 FE3 B:F3S303 0.0 34.1 1.0
S1 B:F3S303 2.2 34.1 1.0
S4 B:F3S303 2.3 34.1 1.0
S3 B:F3S303 2.3 34.1 1.0
FE4 B:F3S303 2.7 34.1 1.0
FE1 B:F3S303 2.7 34.1 1.0
N B:ILE209 2.7 26.6 1.0
SG B:CYS206 3.1 25.9 1.0
CA B:SER208 3.3 26.2 1.0
N B:SER208 3.3 26.2 1.0
C B:SER208 3.3 26.2 1.0
N B:MET210 3.3 27.7 1.0
CA B:ILE209 3.7 26.6 1.0
CB B:ILE209 3.8 26.6 1.0
S2 B:F3S303 4.0 34.1 1.0
C B:ILE209 4.0 26.6 1.0
CG1 B:ILE209 4.2 26.6 1.0
C B:HIS207 4.2 25.9 1.0
N B:HIS207 4.3 25.9 1.0
CA B:MET210 4.3 27.7 1.0
O B:SER208 4.3 26.2 1.0
CB B:CYS206 4.5 25.9 1.0
CB B:SER208 4.8 26.2 1.0
CA B:CYS206 4.8 25.9 1.0
C B:CYS206 4.8 25.9 1.0
CG2 B:THR223 4.8 26.8 1.0
OG1 B:THR223 4.9 26.8 1.0
CA B:HIS207 4.9 25.9 1.0
O B:HIS207 5.0 25.9 1.0

Iron binding site 9 out of 30 in 7jz2

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Iron binding site 9 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:34.1
occ:1.00
 FE4 B:F3S303 0.0 34.1 1.0
S4 B:F3S303 2.3 34.1 1.0
S2 B:F3S303 2.3 34.1 1.0
S3 B:F3S303 2.3 34.1 1.0
FE1 B:F3S303 2.7 34.1 1.0
FE3 B:F3S303 2.7 34.1 1.0
SG B:CYS212 3.3 25.9 1.0
CD1 B:ILE226 3.6 25.0 1.0
SG B:CYS206 3.7 25.9 1.0
S1 B:F3S303 3.9 34.1 1.0
CB B:PRO172 4.3 22.5 1.0
OG1 B:THR223 4.3 26.8 1.0
CB B:CYS212 4.7 25.9 1.0
CA B:THR223 4.8 26.8 1.0
N B:THR223 4.8 26.8 1.0
CB B:CYS206 4.8 25.9 1.0
N B:MET210 4.8 27.7 1.0
CA B:PRO172 5.0 22.5 1.0

Iron binding site 10 out of 30 in 7jz2

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Iron binding site 10 out of 30 in the Succinate: Quinone Oxidoreductase Sqr From E.Coli K12


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Succinate: Quinone Oxidoreductase Sqr From E.Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:22.8
occ:1.00
 FE D:HEM201 0.0 22.8 1.0
NC D:HEM201 2.1 22.8 1.0
NB D:HEM201 2.1 22.8 1.0
ND D:HEM201 2.1 22.8 1.0
NA D:HEM201 2.1 22.8 1.0
NE2 C:HIS84 2.8 23.0 1.0
NE2 D:HIS71 2.8 21.5 1.0
CD2 D:HIS71 2.9 21.5 1.0
C1A D:HEM201 3.0 22.8 1.0
C4A D:HEM201 3.0 22.8 1.0
C4D D:HEM201 3.1 22.8 1.0
C1B D:HEM201 3.1 22.8 1.0
C1C D:HEM201 3.1 22.8 1.0
C1D D:HEM201 3.1 22.8 1.0
C4B D:HEM201 3.1 22.8 1.0
C4C D:HEM201 3.1 22.8 1.0
CHA D:HEM201 3.4 22.8 1.0
CHB D:HEM201 3.4 22.8 1.0
CHC D:HEM201 3.4 22.8 1.0
CHD D:HEM201 3.4 22.8 1.0
CD2 C:HIS84 3.5 23.0 1.0
CE1 D:HIS71 3.8 21.5 1.0
CE1 C:HIS84 3.9 23.0 1.0
CG D:HIS71 4.0 21.5 1.0
C2A D:HEM201 4.2 22.8 1.0
C3A D:HEM201 4.2 22.8 1.0
C3D D:HEM201 4.3 22.8 1.0
C2D D:HEM201 4.3 22.8 1.0
C2B D:HEM201 4.3 22.8 1.0
C2C D:HEM201 4.3 22.8 1.0
C3B D:HEM201 4.3 22.8 1.0
C3C D:HEM201 4.3 22.8 1.0
ND1 D:HIS71 4.4 21.5 1.0
CG C:HIS84 4.7 23.0 1.0
ND1 C:HIS84 4.9 23.0 1.0

Reference:

C.C.Su, M.Lyu, C.E.Morgan, J.R.Bolla, C.V.Robinson, E.W.Yu. A 'Build and Retrieve' Methodology to Simultaneously Solve Cryo-Em Structures of Membrane Proteins. Nat.Methods V. 18 69 2021.
ISSN: ESSN 1548-7105
PubMed: 33408407
DOI: 10.1038/S41592-020-01021-2
Page generated: Wed Aug 6 22:37:00 2025

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