Iron in PDB 6awf: Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate

All present enzymatic activity of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate:
1.3.5.1; 1.3.5.4;

The structure of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate, PDB code: 6awf was solved by T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.91 / 3.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	113.318, 117.986, 125.291, 90.00, 98.80, 90.00
R / Rfree (%)	28.5 / 31.8

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 18;

Binding sites:

The binding sites of Iron atom in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate (pdb code 6awf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate, PDB code: 6awf:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:68.7 occ:1.00 FE1 B:FES301 0.0 68.7 1.0 S1 B:FES301 2.2 72.0 1.0 S2 B:FES301 2.2 0.3 1.0 CB B:CYS65 2.7 0.7 1.0 SG B:CYS77 2.8 72.7 1.0 SG B:CYS65 3.0 0.0 1.0 FE2 B:FES301 3.0 76.2 1.0 CB B:CYS77 3.5 75.9 1.0 CA B:CYS65 3.9 0.2 1.0 N B:CYS65 4.0 0.1 1.0 N B:CYS77 4.6 79.4 1.0 SG B:CYS62 4.6 87.9 1.0 CA B:CYS77 4.7 78.5 1.0 N B:ALA60 4.7 81.2 1.0 N B:ARG58 4.8 95.2 1.0 SG B:CYS57 4.9 0.4 1.0 N B:GLY63 4.9 95.7 1.0 CB B:LEU75 4.9 85.3 1.0 CA B:ALA60 4.9 81.1 1.0 N B:SER64 4.9 0.8 1.0 CD1 B:LEU75 5.0 83.9 1.0

Iron binding site 2 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:76.2 occ:1.00 FE2 B:FES301 0.0 76.2 1.0 S1 B:FES301 2.2 72.0 1.0 S2 B:FES301 2.2 0.3 1.0 SG B:CYS57 2.7 0.4 1.0 SG B:CYS62 2.7 87.9 1.0 CB B:CYS62 2.8 86.8 1.0 FE1 B:FES301 3.0 68.7 1.0 N B:CYS62 3.1 81.5 1.0 CB B:CYS57 3.2 0.2 1.0 CA B:CYS62 3.4 85.5 1.0 N B:CYS57 3.6 95.4 1.0 N B:GLY63 3.6 95.7 1.0 CA B:CYS57 3.8 98.8 1.0 N B:ARG58 3.9 95.2 1.0 C B:CYS62 4.0 89.9 1.0 N B:ILE61 4.1 80.3 1.0 C B:CYS57 4.3 96.8 1.0 C B:ILE61 4.3 78.4 1.0 N B:ALA60 4.4 81.2 1.0 N B:MET59 4.6 93.0 1.0 N B:SER64 4.7 0.8 1.0 C B:SER56 4.7 92.9 1.0 CA B:ALA60 4.8 81.1 1.0 CA B:GLY63 4.8 0.4 1.0 SG B:CYS77 4.8 72.7 1.0 CA B:ILE61 4.8 78.9 1.0 OG B:SER64 4.9 0.5 1.0 N B:SER56 4.9 88.5 1.0 C B:ALA60 4.9 79.9 1.0

Iron binding site 3 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe302 b:58.1 occ:1.00 FE1 B:F3S302 0.0 58.1 1.0 S1 B:F3S302 2.2 66.3 1.0 S2 B:F3S302 2.3 88.5 1.0 S3 B:F3S302 2.3 0.8 1.0 FE4 B:F3S302 2.5 56.7 1.0 FE3 B:F3S302 2.6 56.2 1.0 SG B:CYS204 2.8 70.9 1.0 CB B:CYS204 3.2 71.4 1.0 CA B:CYS204 3.9 72.8 1.0 S4 B:F3S302 4.0 93.6 1.0 N B:PHE206 4.2 71.9 1.0 N B:THR205 4.3 74.0 1.0 CD1 B:ILE224 4.4 64.7 1.0 C B:CYS204 4.4 74.0 1.0 CA B:PHE206 4.5 71.3 1.0 N B:VAL207 4.7 74.0 1.0 SG B:CYS158 4.7 94.4 1.0 SG B:CYS210 4.8 74.1 1.0 CZ B:PHE167 4.8 94.7 1.0

Iron binding site 4 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe302 b:56.2 occ:1.00 FE3 B:F3S302 0.0 56.2 1.0 S1 B:F3S302 2.2 66.3 1.0 S4 B:F3S302 2.2 93.6 1.0 S3 B:F3S302 2.3 0.8 1.0 SG B:CYS210 2.5 74.1 1.0 FE4 B:F3S302 2.5 56.7 1.0 FE1 B:F3S302 2.6 58.1 1.0 CB B:CYS210 3.2 75.1 1.0 S2 B:F3S302 3.9 88.5 1.0 N B:CYS210 4.1 79.1 1.0 N B:GLY208 4.3 77.8 1.0 CA B:CYS210 4.3 77.2 1.0 SG B:CYS158 4.3 94.4 1.0 CB B:PRO170 4.7 89.0 1.0 CA B:GLY208 4.8 81.6 1.0 CB B:CYS158 4.8 93.4 1.0 CD1 B:ILE224 4.8 64.7 1.0 CB B:ALA221 4.9 81.5 1.0 CG B:PRO170 4.9 89.1 1.0 N B:TYR209 5.0 81.7 1.0 N B:VAL207 5.0 74.0 1.0

Iron binding site 5 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe302 b:56.7 occ:1.00 FE4 B:F3S302 0.0 56.7 1.0 S4 B:F3S302 2.2 93.6 1.0 S2 B:F3S302 2.2 88.5 1.0 S3 B:F3S302 2.3 0.8 1.0 SG B:CYS158 2.5 94.4 1.0 FE3 B:F3S302 2.5 56.2 1.0 FE1 B:F3S302 2.5 58.1 1.0 CB B:CYS158 3.7 93.4 1.0 S1 B:F3S302 3.7 66.3 1.0 CA B:CYS158 4.3 94.5 1.0 CB B:GLN160 4.5 90.9 1.0 CG B:GLN160 4.5 89.9 1.0 CB B:VAL207 4.6 73.8 1.0 CE2 B:PHE167 4.6 96.0 1.0 CD B:PRO159 4.7 93.1 1.0 N B:VAL207 4.8 74.0 1.0 SG B:CYS210 4.9 74.1 1.0 C B:CYS158 5.0 94.0 1.0 CB B:CYS204 5.0 71.4 1.0

Iron binding site 6 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe303 b:70.5 occ:1.00 FE1 B:SF4303 0.0 70.5 1.0 S2 B:SF4303 2.2 71.2 1.0 S4 B:SF4303 2.2 71.9 1.0 S3 B:SF4303 2.3 0.5 1.0 SG B:CYS151 2.6 80.2 1.0 FE4 B:SF4303 2.6 57.7 1.0 FE2 B:SF4303 2.7 56.5 1.0 FE3 B:SF4303 2.8 71.9 1.0 N B:CYS151 3.7 81.8 1.0 N B:GLY152 3.7 80.2 1.0 CB B:CYS151 3.9 81.0 1.0 S1 B:SF4303 3.9 88.5 1.0 CA B:CYS151 4.2 81.3 1.0 N B:LEU153 4.4 78.2 1.0 CD B:PRO215 4.4 89.9 1.0 C B:CYS151 4.4 80.0 1.0 N B:ASN150 4.7 82.0 1.0 CA B:GLY152 4.7 81.3 1.0 C B:ASN150 4.7 80.8 1.0 CG B:PRO215 4.9 90.0 1.0 CA B:ASN150 4.9 79.2 1.0 SG B:CYS148 4.9 89.9 1.0 C B:GLY152 4.9 80.5 1.0 CG1 B:ILE149 4.9 86.9 1.0 N B:ILE149 5.0 88.7 1.0 N B:CYS154 5.0 81.0 1.0

Iron binding site 7 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe303 b:56.5 occ:1.00 FE2 B:SF4303 0.0 56.5 1.0 S4 B:SF4303 2.2 71.9 1.0 S1 B:SF4303 2.2 88.5 1.0 S3 B:SF4303 2.3 0.5 1.0 FE3 B:SF4303 2.5 71.9 1.0 FE4 B:SF4303 2.7 57.7 1.0 FE1 B:SF4303 2.7 70.5 1.0 SG B:CYS148 2.8 89.9 1.0 CB B:CYS148 3.3 89.1 1.0 S2 B:SF4303 3.7 71.2 1.0 CA B:CYS148 3.7 89.2 1.0 N B:ILE149 4.3 88.7 1.0 C B:CYS148 4.4 88.1 1.0 CB B:ALA171 4.4 75.5 1.0 N B:ASN150 4.5 82.0 1.0 CA B:ALA171 4.9 77.9 1.0 CA B:ASN150 5.0 79.2 1.0 N B:CYS148 5.0 88.8 1.0 CG2 B:VAL218 5.0 90.2 1.0

Iron binding site 8 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe303 b:71.9 occ:1.00 FE3 B:SF4303 0.0 71.9 1.0 S4 B:SF4303 2.2 71.9 1.0 S2 B:SF4303 2.3 71.2 1.0 S1 B:SF4303 2.3 88.5 1.0 FE2 B:SF4303 2.5 56.5 1.0 FE4 B:SF4303 2.8 57.7 1.0 FE1 B:SF4303 2.8 70.5 1.0 SG B:CYS154 2.9 76.9 1.0 CB B:CYS154 3.7 79.4 1.0 S3 B:SF4303 3.8 0.5 1.0 CB B:ALA171 4.1 75.5 1.0 N B:CYS154 4.4 81.0 1.0 CA B:ALA171 4.5 77.9 1.0 N B:ALA171 4.6 83.9 1.0 CA B:CYS154 4.7 81.4 1.0 SG B:CYS148 4.9 89.9 1.0

Iron binding site 9 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe303 b:57.7 occ:1.00 FE4 B:SF4303 0.0 57.7 1.0 S3 B:SF4303 2.2 0.5 1.0 S1 B:SF4303 2.2 88.5 1.0 S2 B:SF4303 2.3 71.2 1.0 FE1 B:SF4303 2.6 70.5 1.0 FE2 B:SF4303 2.7 56.5 1.0 SG B:CYS214 2.7 91.9 1.0 FE3 B:SF4303 2.8 71.9 1.0 CB B:CYS214 3.4 90.6 1.0 S4 B:SF4303 3.8 71.9 1.0 CA B:CYS214 3.9 88.5 1.0 CD B:PRO215 3.9 89.9 1.0 N B:PRO215 4.5 89.7 1.0 C B:CYS214 4.6 87.9 1.0 SG B:CYS151 4.6 80.2 1.0 CG2 B:VAL218 4.7 90.2 1.0 CB B:VAL218 4.8 88.9 1.0 CG B:PRO215 4.9 90.0 1.0 N B:LYS216 5.0 93.0 1.0

Iron binding site 10 out of 18 in the Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Escherichia Coli Quinol:Fumarate Reductase Crystallized Without Dicarboxylate within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe301 b:79.7 occ:1.00 FE1 F:FES301 0.0 79.7 1.0 S1 F:FES301 2.2 77.8 1.0 S2 F:FES301 2.2 82.7 1.0 CB F:CYS65 2.6 1.0 1.0 SG F:CYS77 2.8 91.8 1.0 SG F:CYS65 3.0 0.5 1.0 CB F:CYS77 3.0 93.0 1.0 FE2 F:FES301 3.1 83.0 1.0 N F:CYS77 3.9 92.6 1.0 CA F:CYS65 3.9 0.7 1.0 CA F:CYS77 4.0 94.2 1.0 N F:CYS65 4.3 0.1 1.0 SG F:CYS57 4.4 0.7 1.0 CB F:LEU75 4.6 91.5 1.0 N F:ALA60 4.6 93.8 1.0 N F:ARG58 4.7 95.0 1.0 CA F:ALA60 4.9 99.4 1.0 C F:CYS77 4.9 96.4 1.0 N F:ALA76 5.0 92.4 1.0

C.A.Starbird, T.M.Tomasiak, P.K.Singh, V.Yankovskaya, E.Maklashina, M.Eisenbach, G.Cecchini, T.M.Iverson. New Crystal Forms of the Integral Membrane Escherichia Coli Quinol:Fumarate Reductase Suggest That Ligands Control Domain Movement. J. Struct. Biol. V. 202 100 2018.
ISSN: ESSN 1095-8657
PubMed: 29158068
DOI: 10.1016/J.JSB.2017.11.004