Iron in PDB 3p4q: Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate

All present enzymatic activity of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate:
1.3.99.1;

The structure of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate, PDB code: 3p4q was solved by T.M.Tomasiak, T.L.Archuleta, J.Andrell, C.Luna-Chavez, T.A.Davis, M.Sarwar, A.J.Ham, W.H.Mcdonald, V.Yankowskaya, H.A.Stern, J.N.Johnston, E.Maklashina, G.Cecchini, T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.57 / 3.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	96.641, 137.964, 272.803, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26.1

Pages:

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

Binding sites:

The binding sites of Iron atom in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate (pdb code 3p4q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate, PDB code: 3p4q:
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 Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe244 b:34.1 occ:1.00 FE1 B:FES244 0.0 34.1 1.0 SG B:CYS65 2.0 40.3 1.0 S1 B:FES244 2.1 35.9 1.0 SG B:CYS77 2.2 47.0 1.0 S2 B:FES244 2.3 32.8 1.0 FE2 B:FES244 3.0 34.7 1.0 CB B:CYS65 3.3 39.0 1.0 CB B:CYS77 3.6 48.1 1.0 CA B:ALA60 3.9 32.0 1.0 SG B:CYS57 4.0 29.2 1.0 N B:ALA60 4.0 31.6 1.0 CD2 B:LEU75 4.1 40.0 1.0 N B:CYS65 4.2 38.4 1.0 N B:CYS77 4.3 47.6 1.0 CA B:CYS65 4.4 39.1 1.0 CB B:LEU75 4.5 40.1 1.0 CA B:CYS77 4.5 48.3 1.0 CB B:ALA60 4.6 32.5 1.0 CD1 B:LEU75 4.6 40.0 1.0 CG B:LEU75 4.6 40.2 1.0 N B:ARG58 4.8 29.4 1.0 C B:ALA60 4.9 32.5 1.0 N B:SER64 4.9 37.3 1.0 SG B:CYS62 4.9 34.4 1.0 N B:ALA76 5.0 40.1 1.0

Iron binding site 2 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe244 b:34.7 occ:1.00 FE2 B:FES244 0.0 34.7 1.0 S2 B:FES244 2.1 32.8 1.0 SG B:CYS62 2.2 34.4 1.0 SG B:CYS57 2.2 29.2 1.0 S1 B:FES244 2.3 35.9 1.0 CB B:CYS57 2.8 29.6 1.0 FE1 B:FES244 3.0 34.1 1.0 N B:CYS57 3.1 29.5 1.0 CB B:CYS62 3.4 34.3 1.0 CA B:CYS57 3.4 29.6 1.0 N B:CYS62 3.6 33.9 1.0 N B:ARG58 3.7 29.4 1.0 N B:GLY63 3.8 35.6 1.0 CA B:CYS62 3.9 34.7 1.0 OG B:SER64 4.0 38.3 1.0 C B:CYS57 4.0 29.6 1.0 SG B:CYS65 4.2 40.3 1.0 C B:SER56 4.2 29.6 1.0 N B:SER56 4.2 30.6 1.0 C B:CYS62 4.3 35.3 1.0 N B:ILE61 4.3 32.8 1.0 N B:SER64 4.4 37.3 1.0 N B:ALA60 4.4 31.6 1.0 CA B:ALA60 4.6 32.0 1.0 CA B:SER56 4.6 30.0 1.0 SG B:CYS77 4.7 47.0 1.0 C B:ILE61 4.8 33.9 1.0 CA B:ARG58 4.8 29.6 1.0 N B:MET59 4.9 30.3 1.0 CA B:GLY63 4.9 36.8 1.0 CB B:SER56 4.9 30.1 1.0 C B:ALA60 4.9 32.5 1.0

Iron binding site 3 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:47.4 occ:1.00 FE1 B:F3S245 0.0 47.4 1.0 SG B:CYS204 2.1 49.3 1.0 S3 B:F3S245 2.2 47.7 1.0 S2 B:F3S245 2.2 47.6 1.0 S1 B:F3S245 2.3 47.1 1.0 FE4 B:F3S245 2.7 47.5 1.0 FE3 B:F3S245 2.7 47.1 1.0 CB B:CYS204 3.1 49.1 1.0 CA B:CYS204 3.8 49.6 1.0 N B:PHE206 3.8 48.6 1.0 S4 B:F3S245 3.9 45.7 1.0 CA B:PHE206 4.1 48.2 1.0 CD1 B:ILE224 4.1 42.7 1.0 N B:VAL207 4.2 47.7 1.0 N B:THR205 4.3 49.6 1.0 C B:CYS204 4.3 49.7 1.0 SG B:CYS158 4.5 46.8 1.0 C B:PHE206 4.7 48.1 1.0 N B:GLY208 4.7 46.9 1.0 SG B:CYS210 4.8 47.6 1.0 CG2 B:ILE224 4.9 43.9 1.0 C B:THR205 4.9 49.2 1.0

Iron binding site 4 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:47.1 occ:1.00 FE3 B:F3S245 0.0 47.1 1.0 S1 B:F3S245 2.2 47.1 1.0 SG B:CYS210 2.2 47.6 1.0 S3 B:F3S245 2.2 47.7 1.0 S4 B:F3S245 2.2 45.7 1.0 FE4 B:F3S245 2.7 47.5 1.0 FE1 B:F3S245 2.7 47.4 1.0 CB B:CYS210 3.4 47.5 1.0 S2 B:F3S245 3.8 47.6 1.0 N B:GLY208 3.9 46.9 1.0 N B:CYS210 4.0 47.5 1.0 CA B:GLY208 4.1 46.9 1.0 CA B:CYS210 4.3 47.7 1.0 N B:TYR209 4.4 47.2 1.0 CD1 B:ILE224 4.4 42.7 1.0 C B:GLY208 4.5 46.9 1.0 SG B:CYS158 4.5 46.8 1.0 CB B:CYS158 4.6 45.0 1.0 SG B:CYS204 4.7 49.3 1.0 CB B:ALA221 4.7 43.5 1.0 CB B:PRO170 4.8 36.1 1.0 CA B:ALA221 4.9 43.2 1.0 N B:VAL207 4.9 47.7 1.0 C B:VAL207 5.0 47.2 1.0

Iron binding site 5 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe245 b:47.5 occ:1.00 FE4 B:F3S245 0.0 47.5 1.0 SG B:CYS158 2.1 46.8 1.0 S2 B:F3S245 2.2 47.6 1.0 S4 B:F3S245 2.3 45.7 1.0 S3 B:F3S245 2.3 47.7 1.0 FE3 B:F3S245 2.7 47.1 1.0 FE1 B:F3S245 2.7 47.4 1.0 CB B:CYS158 3.0 45.0 1.0 CA B:CYS158 3.7 45.5 1.0 S1 B:F3S245 3.9 47.1 1.0 CD B:PRO159 4.1 48.9 1.0 C B:CYS158 4.4 47.3 1.0 CG B:GLN160 4.5 53.5 1.0 N B:PRO159 4.5 48.7 1.0 CB B:GLN160 4.6 52.7 1.0 CG2 B:VAL207 4.6 47.5 1.0 SG B:CYS210 4.6 47.6 1.0 CB B:VAL207 4.6 47.4 1.0 SG B:CYS204 4.7 49.3 1.0 N B:GLN160 4.8 51.6 1.0 CE2 B:PHE167 4.8 48.1 1.0 N B:CYS158 4.9 44.2 1.0 N B:VAL207 5.0 47.7 1.0

Iron binding site 6 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:64.4 occ:1.00 FE1 B:SF4246 0.0 64.4 1.0 SG B:CYS151 1.8 44.6 1.0 S4 B:SF4246 2.0 65.0 1.0 S2 B:SF4246 2.2 64.0 1.0 S3 B:SF4246 2.3 66.4 1.0 FE3 B:SF4246 2.7 64.7 1.0 FE2 B:SF4246 2.7 66.6 1.0 FE4 B:SF4246 2.8 65.7 1.0 CB B:CYS151 3.4 45.6 1.0 N B:GLY152 3.5 43.2 1.0 N B:CYS151 3.6 44.9 1.0 S1 B:SF4246 3.8 65.7 1.0 SG B:CYS154 3.8 39.4 1.0 CA B:CYS151 3.9 45.5 1.0 N B:LEU153 4.1 42.0 1.0 CD B:PRO215 4.1 49.8 1.0 C B:CYS151 4.2 44.7 1.0 SG B:CYS148 4.4 42.7 1.0 CG B:PRO215 4.4 49.6 1.0 N B:ASN150 4.4 44.7 1.0 C B:ASN150 4.5 45.0 1.0 CA B:GLY152 4.5 42.7 1.0 CB B:LEU153 4.6 42.2 1.0 N B:CYS154 4.6 40.2 1.0 SG B:CYS214 4.7 51.3 1.0 C B:GLY152 4.7 42.3 1.0 CA B:ASN150 4.7 44.5 1.0 CG1 B:ILE149 4.8 47.6 1.0 CA B:LEU153 4.8 41.8 1.0 CG B:LEU153 5.0 43.3 1.0

Iron binding site 7 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:66.6 occ:1.00 FE2 B:SF4246 0.0 66.6 1.0 SG B:CYS148 2.0 42.7 1.0 S4 B:SF4246 2.1 65.0 1.0 S1 B:SF4246 2.2 65.7 1.0 S3 B:SF4246 2.2 66.4 1.0 FE3 B:SF4246 2.5 64.7 1.0 FE4 B:SF4246 2.7 65.7 1.0 FE1 B:SF4246 2.7 64.4 1.0 CB B:CYS148 3.3 43.3 1.0 S2 B:SF4246 3.5 64.0 1.0 SG B:CYS154 3.8 39.4 1.0 CA B:CYS148 3.9 44.6 1.0 N B:ASN150 4.1 44.7 1.0 N B:ILE149 4.2 45.8 1.0 CB B:ALA171 4.3 34.9 1.0 C B:CYS148 4.4 45.4 1.0 SG B:CYS151 4.4 44.6 1.0 CA B:ASN150 4.6 44.5 1.0 SG B:CYS214 4.6 51.3 1.0 N B:CYS151 4.8 44.9 1.0 CA B:ALA171 5.0 34.8 1.0

Iron binding site 8 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:64.7 occ:1.00 FE3 B:SF4246 0.0 64.7 1.0 SG B:CYS154 1.5 39.4 1.0 S2 B:SF4246 1.9 64.0 1.0 S1 B:SF4246 2.1 65.7 1.0 S4 B:SF4246 2.3 65.0 1.0 FE2 B:SF4246 2.5 66.6 1.0 FE4 B:SF4246 2.6 65.7 1.0 FE1 B:SF4246 2.7 64.4 1.0 CB B:CYS154 3.1 39.1 1.0 S3 B:SF4246 3.7 66.4 1.0 N B:CYS154 3.7 40.2 1.0 CA B:CYS154 4.0 39.8 1.0 CB B:ALA171 4.1 34.9 1.0 SG B:CYS151 4.3 44.6 1.0 SG B:CYS148 4.3 42.7 1.0 SG B:CYS214 4.6 51.3 1.0 N B:GLY152 4.7 43.2 1.0 CA B:ALA171 4.7 34.8 1.0 N B:LEU153 4.8 42.0 1.0 C B:LEU153 4.9 41.1 1.0 CA B:GLY152 4.9 42.7 1.0 N B:ALA171 4.9 35.2 1.0 C B:GLY152 5.0 42.3 1.0

Iron binding site 9 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe246 b:65.7 occ:1.00 FE4 B:SF4246 0.0 65.7 1.0 S1 B:SF4246 2.1 65.7 1.0 SG B:CYS214 2.1 51.3 1.0 S2 B:SF4246 2.2 64.0 1.0 S3 B:SF4246 2.3 66.4 1.0 FE3 B:SF4246 2.6 64.7 1.0 FE2 B:SF4246 2.7 66.6 1.0 FE1 B:SF4246 2.8 64.4 1.0 CB B:CYS214 3.3 49.8 1.0 CA B:CYS214 3.6 50.2 1.0 S4 B:SF4246 3.7 65.0 1.0 SG B:CYS154 4.0 39.4 1.0 CD B:PRO215 4.1 49.8 1.0 SG B:CYS151 4.3 44.6 1.0 N B:PRO215 4.4 49.7 1.0 C B:CYS214 4.4 50.1 1.0 SG B:CYS148 4.4 42.7 1.0 CB B:VAL218 4.6 43.0 1.0 CG2 B:VAL218 4.6 42.5 1.0 N B:CYS214 4.8 50.4 1.0 CG B:PRO215 4.9 49.6 1.0 N B:LYS216 5.0 48.1 1.0

Iron binding site 10 out of 18 in the Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of Menaquinol:Oxidoreductase in Complex with Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe244 b:82.4 occ:1.00 FE1 N:SF4244 0.0 82.4 1.0 SG N:CYS151 2.0 0.3 1.0 S2 N:SF4244 2.3 82.2 1.0 S3 N:SF4244 2.3 83.2 1.0 S4 N:SF4244 2.3 83.0 1.0 FE4 N:SF4244 2.7 83.2 1.0 FE3 N:SF4244 2.7 82.2 1.0 FE2 N:SF4244 2.7 82.8 1.0 CB N:CYS151 2.8 0.2 1.0 N N:CYS151 3.1 0.7 1.0 CA N:CYS151 3.4 0.1 1.0 N N:GLY152 3.5 0.1 1.0 S1 N:SF4244 3.9 82.2 1.0 C N:CYS151 4.0 0.8 1.0 CG1 N:ILE149 4.2 0.6 1.0 C N:ASN150 4.2 0.9 1.0 N N:LEU153 4.3 1.0 1.0 SG N:CYS214 4.4 91.4 1.0 N N:ASN150 4.4 0.5 1.0 CA N:ASN150 4.6 0.8 1.0 CD N:PRO215 4.6 92.2 1.0 SG N:CYS154 4.6 97.0 1.0 CA N:GLY152 4.6 0.8 1.0 CD1 N:LEU153 4.8 0.9 1.0 SG N:CYS148 4.9 0.5 1.0 C N:ILE149 4.9 0.9 1.0 CD1 N:ILE149 4.9 0.6 1.0 N N:ILE149 4.9 0.1 1.0 C N:GLY152 5.0 1.0 1.0 CB N:LEU153 5.0 0.0 1.0

T.M.Tomasiak, T.L.Archuleta, J.Andrell, C.Luna-Chavez, T.A.Davis, M.Sarwar, A.J.Ham, W.H.Mcdonald, V.Yankovskaya, H.A.Stern, J.N.Johnston, E.Maklashina, G.Cecchini, T.M.Iverson. Geometric Restraint Drives on- and Off-Pathway Catalysis By the Escherichia Coli Menaquinol:Fumarate Reductase. J.Biol.Chem. V. 286 3047 2011.
ISSN: ISSN 0021-9258
PubMed: 21098488
DOI: 10.1074/JBC.M110.192849