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Iron in PDB 3vr8: Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum

Protein crystallography data

The structure of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum, PDB code: 3vr8 was solved by H.Shimizu, T.Shiba, D.K.Inaoka, A.Osanai, K.Kita, K.Sakamoto, S.Harada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.56 / 2.81
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 123.707, 129.090, 221.167, 90.00, 90.00, 90.00
R / Rfree (%) 23.1 / 29.7

Iron Binding Sites:

Pages:

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

Binding sites:

The binding sites of Iron atom in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum (pdb code 3vr8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum, PDB code: 3vr8:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in 3vr8

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Iron binding site 1 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:70.6
occ:1.00
FE1 B:FES301 0.0 70.6 1.0
SG B:CYS97 2.2 74.4 1.0
S1 B:FES301 2.2 72.2 1.0
S2 B:FES301 2.2 70.1 1.0
SG B:CYS109 2.4 79.5 1.0
CB B:CYS97 2.9 75.0 1.0
FE2 B:FES301 2.9 78.1 1.0
CB B:CYS109 3.1 82.3 1.0
N B:CYS97 3.8 75.1 1.0
CA B:CYS97 3.9 75.3 1.0
N B:CYS109 4.2 82.3 1.0
CA B:CYS109 4.3 82.1 1.0
CA B:GLY92 4.4 77.4 1.0
SG B:CYS89 4.5 82.6 1.0
SG B:CYS94 4.5 73.2 1.0
CB B:LEU107 4.5 83.2 1.0
N B:GLY92 4.6 79.9 1.0
C B:CYS97 4.7 76.1 1.0
N B:ARG90 4.7 84.3 1.0
N B:SER96 4.8 72.9 1.0
CD2 B:LEU107 4.9 81.3 1.0

Iron binding site 2 out of 20 in 3vr8

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Iron binding site 2 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:78.1
occ:1.00
FE2 B:FES301 0.0 78.1 1.0
S2 B:FES301 2.2 70.1 1.0
S1 B:FES301 2.2 72.2 1.0
SG B:CYS89 2.3 82.6 1.0
SG B:CYS94 2.3 73.2 1.0
FE1 B:FES301 2.9 70.6 1.0
N B:CYS89 3.3 82.9 1.0
CB B:CYS94 3.3 72.6 1.0
CB B:CYS89 3.3 83.0 1.0
N B:CYS94 3.4 71.8 1.0
CA B:CYS89 3.7 83.0 1.0
CA B:CYS94 3.8 72.1 1.0
N B:GLY95 3.8 72.5 1.0
N B:ARG90 3.9 84.3 1.0
N B:ILE93 3.9 74.2 1.0
N B:GLY92 4.2 79.9 1.0
CA B:GLY92 4.2 77.4 1.0
SG B:CYS109 4.2 79.5 1.0
C B:SER88 4.3 82.3 1.0
N B:SER96 4.3 72.9 1.0
C B:CYS94 4.3 72.3 1.0
C B:CYS89 4.3 83.3 1.0
C B:GLY92 4.5 75.8 1.0
C B:ILE93 4.5 72.2 1.0
N B:SER88 4.5 81.2 1.0
CA B:SER88 4.7 81.7 1.0
CA B:ILE93 4.8 72.8 1.0
CA B:GLY95 4.8 72.6 1.0
CB B:SER88 4.9 81.4 1.0
C B:GLY95 4.9 72.9 1.0
SG B:CYS97 4.9 74.4 1.0

Iron binding site 3 out of 20 in 3vr8

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Iron binding site 3 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:67.6
occ:1.00
FE1 B:SF4302 0.0 67.6 1.0
SG B:CYS185 2.3 75.3 1.0
S4 B:SF4302 2.3 65.5 1.0
S3 B:SF4302 2.3 66.6 1.0
S2 B:SF4302 2.3 64.3 1.0
FE2 B:SF4302 2.6 68.9 1.0
FE4 B:SF4302 2.7 63.4 1.0
FE3 B:SF4302 2.8 71.0 1.0
CB B:CYS185 3.4 76.3 1.0
N B:CYS185 3.6 76.6 1.0
N B:ALA186 3.9 75.6 1.0
S1 B:SF4302 3.9 68.4 1.0
CA B:CYS185 4.0 76.4 1.0
CG1 B:ILE183 4.3 80.6 1.0
N B:CYS187 4.3 75.0 1.0
C B:CYS185 4.4 76.5 1.0
CD B:PRO250 4.4 83.0 1.0
SG B:CYS249 4.5 81.1 1.0
N B:LEU184 4.6 77.8 1.0
CG B:PRO250 4.6 84.0 1.0
SG B:CYS182 4.6 83.1 1.0
SG B:CYS188 4.6 77.3 1.0
C B:LEU184 4.7 76.7 1.0
N B:ILE183 4.8 81.2 1.0
CA B:ALA186 4.8 75.0 1.0
N B:CYS188 4.9 75.6 1.0
CA B:LEU184 4.9 76.9 1.0

Iron binding site 4 out of 20 in 3vr8

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Iron binding site 4 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:68.9
occ:1.00
FE2 B:SF4302 0.0 68.9 1.0
SG B:CYS188 2.1 77.3 1.0
S4 B:SF4302 2.3 65.5 1.0
S3 B:SF4302 2.3 66.6 1.0
S1 B:SF4302 2.3 68.4 1.0
FE1 B:SF4302 2.6 67.6 1.0
FE3 B:SF4302 2.7 71.0 1.0
FE4 B:SF4302 2.7 63.4 1.0
CB B:CYS188 3.2 74.9 1.0
N B:CYS188 3.6 75.6 1.0
S2 B:SF4302 3.8 64.3 1.0
CA B:CYS188 4.0 75.4 1.0
CB B:ALA206 4.2 77.9 1.0
SG B:CYS185 4.4 75.3 1.0
N B:CYS187 4.4 75.0 1.0
CA B:ALA206 4.5 78.1 1.0
N B:ALA186 4.5 75.6 1.0
SG B:CYS182 4.6 83.1 1.0
CA B:ALA186 4.7 75.0 1.0
SG B:CYS249 4.8 81.1 1.0
C B:ALA186 4.8 75.2 1.0
C B:CYS187 4.8 75.8 1.0
N B:SER189 4.9 74.8 1.0
N B:ALA206 5.0 77.6 1.0

Iron binding site 5 out of 20 in 3vr8

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Iron binding site 5 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:71.0
occ:1.00
FE3 B:SF4302 0.0 71.0 1.0
SG B:CYS182 2.2 83.1 1.0
S1 B:SF4302 2.2 68.4 1.0
S2 B:SF4302 2.3 64.3 1.0
S4 B:SF4302 2.3 65.5 1.0
FE2 B:SF4302 2.7 68.9 1.0
FE4 B:SF4302 2.7 63.4 1.0
FE1 B:SF4302 2.8 67.6 1.0
CB B:CYS182 3.5 84.1 1.0
CA B:CYS182 3.9 83.8 1.0
S3 B:SF4302 3.9 66.6 1.0
N B:ILE183 4.0 81.2 1.0
CD1 B:LEU253 4.2 84.7 1.0
N B:LEU184 4.3 77.8 1.0
C B:CYS182 4.4 82.6 1.0
SG B:CYS188 4.5 77.3 1.0
SG B:CYS249 4.7 81.1 1.0
CA B:LEU184 4.8 76.9 1.0
N B:CYS185 4.9 76.6 1.0
SG B:CYS185 4.9 75.3 1.0

Iron binding site 6 out of 20 in 3vr8

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Iron binding site 6 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe302

b:63.4
occ:1.00
FE4 B:SF4302 0.0 63.4 1.0
SG B:CYS249 2.2 81.1 1.0
S2 B:SF4302 2.3 64.3 1.0
S1 B:SF4302 2.3 68.4 1.0
S3 B:SF4302 2.3 66.6 1.0
FE3 B:SF4302 2.7 71.0 1.0
FE2 B:SF4302 2.7 68.9 1.0
FE1 B:SF4302 2.7 67.6 1.0
CB B:CYS249 3.2 82.6 1.0
S4 B:SF4302 3.9 65.5 1.0
CA B:CYS249 4.0 82.7 1.0
CD1 B:LEU253 4.1 84.7 1.0
CD B:PRO250 4.3 83.0 1.0
CB B:LEU253 4.4 85.7 1.0
SG B:CYS188 4.4 77.3 1.0
C B:CYS249 4.6 82.8 1.0
CG B:LEU253 4.7 85.0 1.0
SG B:CYS185 4.7 75.3 1.0
CB B:CYS188 4.7 74.9 1.0
N B:PRO250 4.8 83.2 1.0
SG B:CYS182 4.8 83.1 1.0
CB B:LYS251 5.0 83.4 1.0
N B:LYS251 5.0 83.4 1.0

Iron binding site 7 out of 20 in 3vr8

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Iron binding site 7 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:85.9
occ:1.00
FE1 B:F3S303 0.0 85.9 1.0
S3 B:F3S303 2.1 85.5 1.0
S1 B:F3S303 2.2 86.9 1.0
S2 B:F3S303 2.2 87.2 1.0
SG B:CYS239 2.5 92.0 1.0
FE4 B:F3S303 2.5 86.2 1.0
FE3 B:F3S303 2.5 84.6 1.0
CB B:CYS239 3.6 90.8 1.0
S4 B:F3S303 3.7 83.4 1.0
OH B:TYR202 3.8 76.1 1.0
CA B:CYS239 3.9 90.9 1.0
N B:THR241 4.0 88.3 1.0
CD1 B:ILE259 4.2 86.5 1.0
CA B:THR241 4.2 86.9 1.0
SG B:CYS192 4.3 76.2 1.0
N B:ILE242 4.3 84.9 1.0
N B:HIS240 4.3 90.1 1.0
C B:CYS239 4.4 90.4 1.0
SG B:CYS245 4.5 86.2 1.0
C B:THR241 4.6 86.2 1.0
C B:HIS240 4.9 89.2 1.0
N B:MET243 5.0 83.0 1.0
CZ B:TYR202 5.0 76.6 1.0

Iron binding site 8 out of 20 in 3vr8

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Iron binding site 8 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:84.6
occ:1.00
FE3 B:F3S303 0.0 84.6 1.0
S3 B:F3S303 2.1 85.5 1.0
S1 B:F3S303 2.2 86.9 1.0
S4 B:F3S303 2.2 83.4 1.0
SG B:CYS245 2.3 86.2 1.0
FE1 B:F3S303 2.5 85.9 1.0
FE4 B:F3S303 2.5 86.2 1.0
CB B:CYS245 3.2 83.9 1.0
S2 B:F3S303 3.6 87.2 1.0
N B:CYS245 3.8 83.7 1.0
N B:MET243 4.1 83.0 1.0
CA B:CYS245 4.1 84.0 1.0
SG B:CYS192 4.2 76.2 1.0
CA B:MET243 4.4 83.1 1.0
CB B:CYS192 4.5 77.6 1.0
C B:MET243 4.6 83.4 1.0
CD1 B:ILE259 4.6 86.5 1.0
CB B:PRO205 4.6 77.0 1.0
N B:ASN244 4.8 83.4 1.0
SG B:CYS239 4.8 92.0 1.0
CB B:ALA256 4.8 85.4 1.0
CG B:PRO205 4.8 76.3 1.0
O B:MET243 5.0 84.0 1.0
C B:ASN244 5.0 83.4 1.0

Iron binding site 9 out of 20 in 3vr8

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Iron binding site 9 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:86.2
occ:1.00
FE4 B:F3S303 0.0 86.2 1.0
SG B:CYS192 1.9 76.2 1.0
S3 B:F3S303 2.1 85.5 1.0
S2 B:F3S303 2.2 87.2 1.0
S4 B:F3S303 2.2 83.4 1.0
FE1 B:F3S303 2.5 85.9 1.0
FE3 B:F3S303 2.5 84.6 1.0
CB B:CYS192 3.0 77.6 1.0
S1 B:F3S303 3.7 86.9 1.0
CA B:CYS192 4.0 77.5 1.0
OH B:TYR202 4.2 76.1 1.0
C B:CYS192 4.6 78.0 1.0
CE2 B:TYR202 4.6 77.9 1.0
CB B:SER194 4.7 81.0 1.0
CD1 B:ILE242 4.7 80.7 1.0
CB B:ILE242 4.7 83.9 1.0
SG B:CYS245 4.7 86.2 1.0
CD B:PRO205 4.8 77.3 1.0
SG B:CYS239 4.9 92.0 1.0
N B:ILE242 4.9 84.9 1.0
CG1 B:ILE242 4.9 83.4 1.0
CZ B:TYR202 5.0 76.6 1.0

Iron binding site 10 out of 20 in 3vr8

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Iron binding site 10 out of 20 in the Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Mitochondrial Rhodoquinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:93.0
occ:1.00
FE C:HEM201 0.0 93.0 1.0
NA C:HEM201 2.0 93.0 1.0
NE2 C:HIS131 2.0 89.6 1.0
NC C:HEM201 2.0 94.5 1.0
NB C:HEM201 2.0 92.9 1.0
NE2 D:HIS95 2.0 90.8 1.0
ND C:HEM201 2.1 93.7 1.0
CE1 D:HIS95 2.9 91.1 1.0
CD2 C:HIS131 2.9 90.1 1.0
C1A C:HEM201 3.0 93.6 1.0
C4B C:HEM201 3.0 94.0 1.0
C1C C:HEM201 3.0 95.3 1.0
CE1 C:HIS131 3.0 89.9 1.0
C4C C:HEM201 3.1 95.0 1.0
C4A C:HEM201 3.1 92.1 1.0
C1B C:HEM201 3.1 92.1 1.0
C4D C:HEM201 3.1 93.6 1.0
CD2 D:HIS95 3.1 91.6 1.0
C1D C:HEM201 3.1 93.4 1.0
CHA C:HEM201 3.3 94.2 1.0
CHC C:HEM201 3.4 94.7 1.0
CHD C:HEM201 3.5 94.2 1.0
CHB C:HEM201 3.5 91.8 1.0
ND1 D:HIS95 4.1 92.2 1.0
ND1 C:HIS131 4.1 90.8 1.0
CG C:HIS131 4.1 90.8 1.0
CG D:HIS95 4.2 93.2 1.0
C2A C:HEM201 4.2 93.2 1.0
C3B C:HEM201 4.2 94.2 1.0
C2C C:HEM201 4.3 95.1 1.0
C3C C:HEM201 4.3 95.9 1.0
C3A C:HEM201 4.3 91.8 1.0
C2B C:HEM201 4.3 92.9 1.0
C2D C:HEM201 4.4 92.4 1.0
C3D C:HEM201 4.4 92.5 1.0
NE2 C:HIS75 4.8 89.2 1.0
CE1 C:HIS75 4.8 88.8 1.0

Reference:

H.Shimizu, A.Osanai, K.Sakamoto, D.K.Inaoka, T.Shiba, S.Harada, K.Kita. Crystal Structure of Mitochondrial Quinol-Fumarate Reductase From the Parasitic Nematode Ascaris Suum J.Biochem. V. 151 589 2012.
ISSN: ISSN 0021-924X
PubMed: 22577165
DOI: 10.1093/JB/MVS051
Page generated: Sun Aug 4 22:08:35 2024

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