Iron in PDB 1l0v: Quinol-Fumarate Reductase with Menaquinol Molecules

All present enzymatic activity of Quinol-Fumarate Reductase with Menaquinol Molecules:
1.3.99.1;

The structure of Quinol-Fumarate Reductase with Menaquinol Molecules, PDB code: 1l0v was solved by T.M.Iverson, C.Luna-Chavez, L.R.Croal, G.Cecchini, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	96.590, 138.090, 275.250, 90.00, 90.00, 90.00
R / Rfree (%)	24.5 / 29

Pages:

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

Binding sites:

The binding sites of Iron atom in the Quinol-Fumarate Reductase with Menaquinol Molecules (pdb code 1l0v). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the Quinol-Fumarate Reductase with Menaquinol Molecules, PDB code: 1l0v:
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 Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe244 b:16.6 occ:1.00 FE1 B:FES244 0.0 16.6 1.0 SG B:CYS65 2.2 34.8 1.0 S2 B:FES244 2.2 16.6 1.0 SG B:CYS77 2.3 19.0 1.0 S1 B:FES244 2.3 16.6 1.0 FE2 B:FES244 2.7 16.6 1.0 CB B:CYS65 3.1 34.8 1.0 CB B:CYS77 3.4 19.0 1.0 CA B:CYS65 4.0 25.1 1.0 N B:CYS65 4.1 25.1 1.0 N B:ALA60 4.1 22.9 1.0 SG B:CYS57 4.2 9.7 1.0 N B:CYS77 4.3 17.6 1.0 CA B:ALA60 4.3 22.9 1.0 CA B:CYS77 4.4 17.6 1.0 SG B:CYS62 4.7 10.7 1.0 N B:ARG58 4.7 11.2 1.0 CB B:LEU75 4.7 16.6 1.0 N B:GLY63 4.9 20.6 1.0 N B:MET59 4.9 21.5 1.0 N B:SER64 5.0 16.8 1.0 CD1 B:LEU75 5.0 16.6 1.0

Iron binding site 2 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe244 b:16.6 occ:1.00 FE2 B:FES244 0.0 16.6 1.0 SG B:CYS62 2.2 10.7 1.0 S2 B:FES244 2.3 16.6 1.0 S1 B:FES244 2.3 16.6 1.0 SG B:CYS57 2.3 9.7 1.0 FE1 B:FES244 2.7 16.6 1.0 CB B:CYS62 3.4 10.7 1.0 N B:GLY63 3.5 20.6 1.0 CB B:CYS57 3.5 9.7 1.0 N B:CYS57 3.5 13.7 1.0 N B:CYS62 3.6 10.7 1.0 CA B:CYS62 3.9 10.7 1.0 CA B:CYS57 3.9 13.7 1.0 N B:ARG58 4.0 11.2 1.0 C B:CYS62 4.2 16.6 1.0 N B:ILE61 4.2 18.6 1.0 N B:SER64 4.2 16.8 1.0 N B:ALA60 4.3 22.9 1.0 SG B:CYS77 4.4 19.0 1.0 N B:SER56 4.4 14.7 1.0 C B:CYS57 4.5 9.7 1.0 OG B:SER64 4.5 62.4 1.0 CA B:GLY63 4.5 20.6 1.0 C B:SER56 4.6 14.7 1.0 CA B:ALA60 4.6 22.9 1.0 SG B:CYS65 4.7 34.8 1.0 N B:MET59 4.7 21.5 1.0 C B:ILE61 4.7 18.6 1.0 N B:CYS65 4.8 25.1 1.0 C B:GLY63 4.8 20.6 1.0 CA B:SER56 4.9 14.7 1.0 C B:ALA60 4.9 22.9 1.0

Iron binding site 3 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:11.7 occ:1.00 FE1 B:F3S245 0.0 11.7 1.0 S2 B:F3S245 2.2 11.7 1.0 SG B:CYS204 2.2 16.6 1.0 S1 B:F3S245 2.3 11.7 1.0 S3 B:F3S245 2.3 11.7 1.0 FE4 B:F3S245 2.6 11.7 1.0 FE3 B:F3S245 2.7 11.7 1.0 CB B:CYS204 3.4 16.6 1.0 S4 B:F3S245 3.8 11.7 1.0 N B:PHE206 3.8 38.5 1.0 CA B:PHE206 4.0 38.5 1.0 N B:VAL207 4.1 17.9 1.0 CD1 B:ILE224 4.1 16.6 1.0 CA B:CYS204 4.1 20.4 1.0 N B:THR205 4.4 22.6 1.0 C B:CYS204 4.5 20.4 1.0 C B:PHE206 4.6 38.5 1.0 SG B:CYS158 4.7 16.6 1.0 N B:GLY208 4.7 22.1 1.0 SG B:CYS210 4.8 16.6 1.0 C B:THR205 4.9 22.6 1.0

Iron binding site 4 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:11.7 occ:1.00 FE3 B:F3S245 0.0 11.7 1.0 S4 B:F3S245 2.2 11.7 1.0 S1 B:F3S245 2.2 11.7 1.0 S3 B:F3S245 2.3 11.7 1.0 SG B:CYS210 2.3 16.6 1.0 FE4 B:F3S245 2.6 11.7 1.0 FE1 B:F3S245 2.7 11.7 1.0 CB B:CYS210 3.4 16.6 1.0 S2 B:F3S245 3.8 11.7 1.0 N B:CYS210 4.0 16.6 1.0 N B:GLY208 4.0 22.1 1.0 CA B:GLY208 4.2 22.1 1.0 CA B:CYS210 4.3 16.6 1.0 C B:GLY208 4.5 22.1 1.0 CD1 B:ILE224 4.5 16.6 1.0 N B:TYR209 4.5 16.6 1.0 SG B:CYS158 4.7 16.6 1.0 CB B:ALA221 4.7 16.6 1.0 SG B:CYS204 4.7 16.6 1.0 CA B:ALA221 4.9 16.6 1.0 N B:VAL207 4.9 17.9 1.0 CB B:CYS158 4.9 16.6 1.0 CB B:PRO170 5.0 16.6 1.0

Iron binding site 5 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:11.7 occ:1.00 FE4 B:F3S245 0.0 11.7 1.0 S3 B:F3S245 2.2 11.7 1.0 SG B:CYS158 2.3 16.6 1.0 S4 B:F3S245 2.3 11.7 1.0 S2 B:F3S245 2.3 11.7 1.0 FE3 B:F3S245 2.6 11.7 1.0 FE1 B:F3S245 2.6 11.7 1.0 CB B:CYS158 3.2 16.6 1.0 S1 B:F3S245 3.8 11.7 1.0 CA B:CYS158 3.9 16.6 1.0 CD B:PRO159 4.4 39.6 1.0 SG B:CYS204 4.6 16.6 1.0 C B:CYS158 4.6 16.6 1.0 CB B:GLN160 4.7 23.7 1.0 SG B:CYS210 4.7 16.6 1.0 CB B:VAL207 4.8 28.3 1.0 CE2 B:PHE167 4.8 21.0 1.0 N B:PRO159 4.8 17.0 1.0 CG B:GLN160 4.8 23.7 1.0 N B:VAL207 4.9 17.9 1.0 N B:GLN160 4.9 30.1 1.0 N B:CYS158 5.0 16.6 1.0

Iron binding site 6 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:2.8 occ:1.00 FE1 B:SF4246 0.0 2.8 1.0 S3 B:SF4246 2.2 2.8 1.0 S4 B:SF4246 2.2 2.8 1.0 SG B:CYS151 2.3 16.6 1.0 S2 B:SF4246 2.3 2.8 1.0 FE2 B:SF4246 2.7 2.8 1.0 FE4 B:SF4246 2.7 2.8 1.0 FE3 B:SF4246 2.8 2.8 1.0 CB B:CYS151 3.6 16.6 1.0 N B:CYS151 3.7 16.6 1.0 N B:GLY152 3.8 43.0 1.0 S1 B:SF4246 3.9 2.8 1.0 CA B:CYS151 4.0 16.6 1.0 CD B:PRO215 4.1 16.6 1.0 N B:LEU153 4.1 16.6 1.0 C B:CYS151 4.4 16.6 1.0 CG B:PRO215 4.5 16.6 1.0 SG B:CYS154 4.6 16.6 1.0 CB B:LEU153 4.6 22.8 1.0 CG1 B:ILE149 4.7 16.6 1.0 C B:ASN150 4.7 16.6 1.0 N B:CYS154 4.7 16.6 1.0 N B:ASN150 4.7 16.6 1.0 CA B:GLY152 4.7 43.0 1.0 SG B:CYS214 4.8 16.6 1.0 SG B:CYS148 4.8 16.6 1.0 C B:GLY152 4.8 43.0 1.0 CA B:LEU153 4.9 16.6 1.0 CG B:LEU153 4.9 22.8 1.0 CA B:ASN150 5.0 16.6 1.0

Iron binding site 7 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:2.8 occ:1.00 FE2 B:SF4246 0.0 2.8 1.0 S1 B:SF4246 2.2 2.8 1.0 S3 B:SF4246 2.2 2.8 1.0 SG B:CYS154 2.3 16.6 1.0 S4 B:SF4246 2.3 2.8 1.0 FE4 B:SF4246 2.5 2.8 1.0 FE3 B:SF4246 2.6 2.8 1.0 FE1 B:SF4246 2.7 2.8 1.0 CB B:CYS154 3.3 16.6 1.0 S2 B:SF4246 3.7 2.8 1.0 N B:CYS154 3.9 16.6 1.0 CA B:CYS154 4.2 16.6 1.0 CB B:ALA171 4.3 43.9 1.0 SG B:CYS214 4.6 16.6 1.0 SG B:CYS148 4.6 16.6 1.0 SG B:CYS151 4.7 16.6 1.0 N B:LEU153 4.8 16.6 1.0 CA B:ALA171 4.9 27.3 1.0 N B:GLY152 4.9 43.0 1.0 C B:LEU153 5.0 16.6 1.0

Iron binding site 8 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:2.8 occ:1.00 FE3 B:SF4246 0.0 2.8 1.0 S1 B:SF4246 2.2 2.8 1.0 S4 B:SF4246 2.3 2.8 1.0 S2 B:SF4246 2.3 2.8 1.0 SG B:CYS148 2.3 16.6 1.0 FE2 B:SF4246 2.6 2.8 1.0 FE4 B:SF4246 2.7 2.8 1.0 FE1 B:SF4246 2.8 2.8 1.0 CB B:CYS148 3.4 16.6 1.0 CA B:CYS148 3.9 16.6 1.0 S3 B:SF4246 3.9 2.8 1.0 N B:ASN150 4.1 16.6 1.0 N B:ILE149 4.1 32.3 1.0 C B:CYS148 4.3 16.6 1.0 CB B:ALA171 4.4 43.9 1.0 SG B:CYS214 4.5 16.6 1.0 SG B:CYS154 4.5 16.6 1.0 CA B:ASN150 4.6 16.6 1.0 N B:CYS151 4.7 16.6 1.0 CG2 B:VAL218 4.9 37.3 1.0 SG B:CYS151 4.9 16.6 1.0 C B:ILE149 5.0 32.3 1.0

Iron binding site 9 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:2.8 occ:1.00 FE4 B:SF4246 0.0 2.8 1.0 S2 B:SF4246 2.3 2.8 1.0 SG B:CYS214 2.3 16.6 1.0 S1 B:SF4246 2.3 2.8 1.0 S3 B:SF4246 2.4 2.8 1.0 FE2 B:SF4246 2.5 2.8 1.0 FE3 B:SF4246 2.7 2.8 1.0 FE1 B:SF4246 2.7 2.8 1.0 CB B:CYS214 3.2 16.6 1.0 CA B:CYS214 3.5 16.6 1.0 S4 B:SF4246 3.8 2.8 1.0 CD B:PRO215 4.1 16.6 1.0 CG2 B:VAL218 4.3 37.3 1.0 C B:CYS214 4.4 16.6 1.0 N B:PRO215 4.5 16.6 1.0 CB B:VAL218 4.6 37.3 1.0 SG B:CYS154 4.6 16.6 1.0 N B:CYS214 4.7 16.6 1.0 SG B:CYS151 4.7 16.6 1.0 SG B:CYS148 4.8 16.6 1.0 CD B:PRO220 5.0 16.6 1.0 CG B:PRO215 5.0 16.6 1.0

Iron binding site 10 out of 18 in the Quinol-Fumarate Reductase with Menaquinol Molecules


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Quinol-Fumarate Reductase with Menaquinol Molecules within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe244 b:8.9 occ:1.00 FE1 N:FES244 0.0 8.9 1.0 S2 N:FES244 2.3 8.9 1.0 SG N:CYS77 2.3 44.1 1.0 S1 N:FES244 2.3 8.9 1.0 SG N:CYS65 2.3 41.6 1.0 FE2 N:FES244 2.7 8.9 1.0 CB N:CYS77 3.3 44.1 1.0 CB N:CYS65 3.4 41.6 1.0 N N:CYS65 4.1 58.5 1.0 SG N:CYS57 4.3 79.8 1.0 CA N:CYS65 4.3 58.5 1.0 N N:CYS77 4.4 58.8 1.0 N N:ALA60 4.4 42.1 1.0 CA N:CYS77 4.5 58.8 1.0 CA N:ALA60 4.6 42.1 1.0 N N:ARG58 4.6 70.3 1.0 CB N:LEU75 4.7 21.8 1.0 SG N:CYS62 4.7 48.9 1.0 CA N:ARG58 4.9 70.3 1.0 CD2 N:LEU37 4.9 93.7 1.0 N N:SER64 4.9 55.8 1.0 N N:MET59 5.0 84.5 1.0

T.M.Iverson, C.Luna-Chavez, L.R.Croal, G.Cecchini, D.C.Rees. Crystallographic Studies of the Escherichia Coli Quinol-Fumarate Reductase with Inhibitors Bound to the Quinol-Binding Site. J.Biol.Chem. V. 277 16124 2002.
ISSN: ISSN 0021-9258
PubMed: 11850430
DOI: 10.1074/JBC.M200815200