Iron in PDB 5kkz: Rhodobacter Sphaeroides BC1 with Famoxadone

All present enzymatic activity of Rhodobacter Sphaeroides BC1 with Famoxadone:
1.10.2.2;

The structure of Rhodobacter Sphaeroides BC1 with Famoxadone, PDB code: 5kkz was solved by D.Xia, L.Esser, F.Zhou, W.K.Tang, C.A.Yu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.98 / 2.97
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	120.773, 128.277, 128.283, 63.92, 88.63, 63.38
R / Rfree (%)	21.5 / 25.8

The structure of Rhodobacter Sphaeroides BC1 with Famoxadone also contains other interesting chemical elements:

Strontium

(Sr)

6 atoms

Pages:

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

Binding sites:

The binding sites of Iron atom in the Rhodobacter Sphaeroides BC1 with Famoxadone (pdb code 5kkz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the Rhodobacter Sphaeroides BC1 with Famoxadone, PDB code: 5kkz:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:51.8 occ:1.00 FE A:HEM1001 0.0 51.8 1.0 ND A:HEM1001 1.9 51.6 1.0 NC A:HEM1001 1.9 51.7 1.0 NE2 A:HIS97 2.0 52.1 1.0 NA A:HEM1001 2.0 52.0 1.0 NE2 A:HIS198 2.0 51.6 1.0 NB A:HEM1001 2.1 52.1 1.0 C1D A:HEM1001 2.9 51.5 1.0 CE1 A:HIS198 2.9 51.7 1.0 CE1 A:HIS97 2.9 52.2 1.0 C4C A:HEM1001 2.9 51.5 1.0 HE1 A:HIS198 3.0 61.5 1.0 C4D A:HEM1001 3.0 51.6 1.0 C1C A:HEM1001 3.0 51.8 1.0 CD2 A:HIS97 3.0 52.2 1.0 C1A A:HEM1001 3.0 51.9 1.0 C4A A:HEM1001 3.0 52.2 1.0 HE1 A:HIS97 3.1 62.0 1.0 C1B A:HEM1001 3.1 52.3 1.0 CD2 A:HIS198 3.1 51.4 1.0 C4B A:HEM1001 3.1 52.2 1.0 CHD A:HEM1001 3.2 51.4 1.0 HD2 A:HIS97 3.2 62.1 1.0 HD2 A:HIS198 3.4 61.0 1.0 CHB A:HEM1001 3.4 52.3 1.0 CHA A:HEM1001 3.4 51.8 1.0 CHC A:HEM1001 3.4 52.0 1.0 ND1 A:HIS97 4.1 52.4 1.0 ND1 A:HIS198 4.1 51.5 1.0 C2D A:HEM1001 4.1 51.4 1.0 CG A:HIS97 4.1 52.4 1.0 C3C A:HEM1001 4.2 51.5 1.0 HA3 A:GLY146 4.2 61.3 1.0 CG A:HIS198 4.2 51.3 1.0 HHD A:HEM1001 4.2 61.1 1.0 C3D A:HEM1001 4.2 51.5 1.0 C2C A:HEM1001 4.2 51.6 1.0 C2A A:HEM1001 4.3 52.1 1.0 C3A A:HEM1001 4.3 52.3 1.0 C2B A:HEM1001 4.3 52.5 1.0 C3B A:HEM1001 4.4 52.4 1.0 HHA A:HEM1001 4.4 61.5 1.0 HHB A:HEM1001 4.4 62.2 1.0 HHC A:HEM1001 4.4 61.8 1.0 HA2 A:GLY62 4.6 61.6 1.0 HA2 A:GLY146 4.6 61.3 1.0 HA3 A:GLY62 4.6 61.6 1.0 HE21 A:GLN58 4.8 62.9 1.0 HD12 A:LEU149 4.8 60.7 1.0 CA A:GLY146 4.9 51.6 1.0 HG22 A:THR142 5.0 61.9 1.0

Iron binding site 2 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:56.9 occ:1.00 FE A:HEM1002 0.0 56.9 1.0 NA A:HEM1002 1.9 57.2 1.0 NB A:HEM1002 2.0 56.2 1.0 ND A:HEM1002 2.0 57.6 1.0 NE2 A:HIS212 2.1 56.8 1.0 NC A:HEM1002 2.1 56.7 1.0 NE2 A:HIS111 2.2 57.1 1.0 C4A A:HEM1002 2.8 56.9 1.0 C1B A:HEM1002 2.9 56.1 1.0 C1A A:HEM1002 3.0 57.7 1.0 C4D A:HEM1002 3.0 58.1 1.0 CD2 A:HIS111 3.1 56.9 1.0 CE1 A:HIS212 3.1 56.9 1.0 C4B A:HEM1002 3.1 55.8 1.0 C1D A:HEM1002 3.1 57.8 1.0 CD2 A:HIS212 3.1 56.5 1.0 C1C A:HEM1002 3.2 56.2 1.0 C4C A:HEM1002 3.2 57.0 1.0 HD2 A:HIS111 3.2 67.7 1.0 CHB A:HEM1002 3.2 56.4 1.0 CE1 A:HIS111 3.2 57.5 1.0 HE1 A:HIS212 3.2 67.7 1.0 HD2 A:HIS212 3.3 67.2 1.0 CHA A:HEM1002 3.4 58.1 1.0 HE1 A:HIS111 3.4 68.4 1.0 CHD A:HEM1002 3.5 57.5 1.0 CHC A:HEM1002 3.5 55.8 1.0 C3A A:HEM1002 4.1 57.2 1.0 HHB A:HEM1002 4.1 67.0 1.0 C2A A:HEM1002 4.2 57.7 1.0 C2B A:HEM1002 4.2 55.6 1.0 ND1 A:HIS212 4.2 56.7 1.0 C3D A:HEM1002 4.3 58.6 1.0 CG A:HIS111 4.3 57.2 1.0 CG A:HIS212 4.3 56.4 1.0 C3B A:HEM1002 4.3 55.4 1.0 ND1 A:HIS111 4.3 57.5 1.0 C2D A:HEM1002 4.3 58.4 1.0 HHA A:HEM1002 4.3 69.2 1.0 C2C A:HEM1002 4.4 56.3 1.0 C3C A:HEM1002 4.4 56.7 1.0 HHD A:HEM1002 4.4 68.4 1.0 HHC A:HEM1002 4.5 66.4 1.0 HH22 A:ARG114 4.6 69.9 1.0 HD13 A:LEU51 4.7 66.6 1.0 HD12 A:LEU51 4.7 66.6 1.0 HA2 A:GLY48 4.7 71.7 1.0 HH21 A:ARG114 5.0 69.9 1.0

Iron binding site 3 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1001 b:54.1 occ:1.00 FE B:HEC1001 0.0 54.1 1.0 NE2 B:HIS40 1.9 52.3 1.0 NB B:HEC1001 2.0 53.6 1.0 NC B:HEC1001 2.0 54.6 1.0 NA B:HEC1001 2.0 53.8 1.0 ND B:HEC1001 2.1 54.9 1.0 SD B:MET185 2.2 56.4 1.0 CE1 B:HIS40 2.8 51.8 1.0 HE1 B:HIS40 2.9 62.1 1.0 C1A B:HEC1001 3.0 54.3 1.0 C4B B:HEC1001 3.0 53.9 1.0 C1C B:HEC1001 3.0 54.7 1.0 C4D B:HEC1001 3.0 55.3 1.0 CD2 B:HIS40 3.0 51.7 1.0 C1B B:HEC1001 3.1 53.3 1.0 C4C B:HEC1001 3.1 55.4 1.0 C1D B:HEC1001 3.1 55.6 1.0 C4A B:HEC1001 3.1 53.5 1.0 HD2 B:HIS40 3.3 61.9 1.0 CHA B:HEC1001 3.3 55.0 1.0 CHC B:HEC1001 3.3 54.4 1.0 CHB B:HEC1001 3.5 53.2 1.0 CHD B:HEC1001 3.5 55.8 1.0 CE B:MET185 3.5 56.3 1.0 CG B:MET185 3.5 58.6 1.0 HE1 B:MET185 3.5 66.9 1.0 HG3 B:MET185 3.6 69.7 1.0 HB2 B:MET185 3.6 71.3 1.0 HE2 B:MET185 3.8 66.9 1.0 ND1 B:HIS40 3.9 50.9 1.0 CG B:HIS40 4.1 51.1 1.0 CB B:MET185 4.1 60.0 1.0 C3B B:HEC1001 4.2 53.7 1.0 C2C B:HEC1001 4.2 55.5 1.0 C2A B:HEC1001 4.2 54.4 1.0 C2B B:HEC1001 4.3 53.3 1.0 C3C B:HEC1001 4.3 55.9 1.0 HE3 B:MET185 4.3 66.9 1.0 HHA B:HEC1001 4.3 65.4 1.0 HG2 B:MET185 4.3 69.7 1.0 C3D B:HEC1001 4.3 56.4 1.0 HHC B:HEC1001 4.3 64.7 1.0 C3A B:HEC1001 4.3 53.9 1.0 C2D B:HEC1001 4.3 56.5 1.0 HHB B:HEC1001 4.5 63.3 1.0 HHD B:HEC1001 4.5 66.3 1.0 HB3 B:MET185 4.5 71.3 1.0 HD2 B:PRO98 4.6 64.5 1.0 HD11 B:LEU100 4.7 65.2 1.0 HD21 B:LEU100 4.7 64.5 1.0 HB1 B:ALA97 4.7 65.3 1.0 HG3 B:PRO188 4.8 67.0 1.0 HB2 B:CYS39 4.9 64.0 1.0

Iron binding site 4 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1001 b:83.2 occ:1.00 FE1 C:FES1001 0.0 83.2 1.0 S1 C:FES1001 2.2 87.3 1.0 S2 C:FES1001 2.2 82.2 1.0 SG C:CYS149 2.3 80.2 1.0 SG C:CYS129 2.3 76.5 1.0 HB3 C:CYS129 2.9 89.1 1.0 CB C:CYS129 3.0 74.2 1.0 FE2 C:FES1001 3.1 82.8 1.0 HB2 C:CYS129 3.1 89.1 1.0 HB3 C:HIS131 3.2 82.1 1.0 HB2 C:CYS134 3.2 79.5 1.0 HB3 C:CYS149 3.3 0.1 1.0 HB2 C:CYS151 3.3 98.6 1.0 CB C:CYS149 3.4 84.1 1.0 HB2 C:CYS149 3.7 0.1 1.0 H C:LEU132 3.9 77.5 1.0 H C:HIS152 3.9 0.4 1.0 H C:CYS134 4.0 76.8 1.0 HB2 C:SER154 4.0 96.8 1.0 CB C:HIS131 4.1 68.8 1.0 H C:HIS131 4.2 82.3 1.0 CB C:CYS134 4.2 66.7 1.0 HB2 C:HIS131 4.2 82.1 1.0 H C:CYS151 4.3 0.8 1.0 CB C:CYS151 4.3 82.1 1.0 CA C:CYS129 4.5 71.3 1.0 HG C:SER154 4.5 96.0 1.0 H C:SER154 4.5 0.6 1.0 HB3 C:CYS151 4.6 98.6 1.0 N C:CYS134 4.6 64.5 1.0 HB3 C:CYS134 4.6 79.5 1.0 HH C:TYR156 4.6 0.2 1.0 N C:HIS152 4.6 92.8 1.0 H C:GLY133 4.7 93.1 1.0 CA C:CYS149 4.7 85.6 1.0 N C:LEU132 4.7 65.1 1.0 OG C:SER154 4.8 79.9 1.0 HB2 C:HIS152 4.8 0.5 1.0 ND1 C:HIS131 4.8 70.5 1.0 HA C:CYS129 4.8 85.6 1.0 HG3 C:PRO136 4.8 89.5 1.0 CB C:SER154 4.8 80.5 1.0 HB2 C:ALA167 4.9 0.1 1.0 N C:HIS131 4.9 68.5 1.0 CA C:CYS134 4.9 65.4 1.0 ND1 C:HIS152 4.9 81.2 1.0 C C:CYS129 4.9 73.7 1.0 N C:CYS151 5.0 91.4 1.0 CG C:HIS131 5.0 69.5 1.0

Iron binding site 5 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1001 b:82.8 occ:1.00 FE2 C:FES1001 0.0 82.8 1.0 ND1 C:HIS131 2.1 70.5 1.0 ND1 C:HIS152 2.1 81.2 1.0 S2 C:FES1001 2.2 82.2 1.0 S1 C:FES1001 2.2 87.3 1.0 HB3 C:HIS131 2.6 82.1 1.0 HB2 C:HIS152 2.6 0.5 1.0 CG C:HIS131 3.0 69.5 1.0 CG C:HIS152 3.0 84.3 1.0 FE1 C:FES1001 3.1 83.2 1.0 CE1 C:HIS131 3.2 70.7 1.0 CE1 C:HIS152 3.2 80.6 1.0 CB C:HIS131 3.2 68.8 1.0 CB C:HIS152 3.3 89.5 1.0 HE1 C:HIS131 3.4 84.9 1.0 HE1 C:HIS152 3.4 96.8 1.0 H C:LEU132 3.5 77.5 1.0 H C:HIS152 3.6 0.4 1.0 HB2 C:HIS131 3.6 82.1 1.0 HB2 C:LEU132 3.7 76.0 1.0 HB2 C:CYS151 3.7 98.6 1.0 N C:HIS152 3.8 92.8 1.0 HB3 C:CYS151 3.8 98.6 1.0 HG2 C:PRO166 4.0 0.8 1.0 HB3 C:HIS152 4.0 0.5 1.0 CA C:HIS152 4.1 93.1 1.0 N C:LEU132 4.1 65.1 1.0 HD12 C:LEU132 4.1 77.7 1.0 CD2 C:HIS131 4.2 69.9 1.0 CB C:CYS151 4.2 82.1 1.0 CD2 C:HIS152 4.2 84.0 1.0 NE2 C:HIS131 4.2 70.1 1.0 HG C:LEU132 4.2 76.9 1.0 NE2 C:HIS152 4.2 82.3 1.0 C C:CYS151 4.4 88.6 1.0 CB C:LEU132 4.5 63.9 1.0 HB2 C:PRO166 4.5 0.4 1.0 CA C:HIS131 4.5 67.4 1.0 C C:HIS131 4.7 65.6 1.0 CG C:LEU132 4.7 64.5 1.0 SG C:CYS129 4.7 76.5 1.0 HD2 C:PRO166 4.8 0.4 1.0 C C:HIS152 4.8 96.5 1.0 CA C:LEU132 4.8 63.5 1.0 CD1 C:LEU132 4.9 65.2 1.0 CG C:PRO166 4.9 93.1 1.0 HA C:HIS152 4.9 0.8 1.0 CA C:CYS151 4.9 87.7 1.0 H C:HIS131 5.0 82.3 1.0 SG C:CYS149 5.0 80.2 1.0 HD2 C:HIS131 5.0 84.0 1.0

Iron binding site 6 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe1001 b:47.6 occ:1.00 FE E:HEM1001 0.0 47.6 1.0 NA E:HEM1001 1.9 47.8 1.0 NE2 E:HIS198 2.0 46.9 1.0 NC E:HEM1001 2.0 47.5 1.0 NB E:HEM1001 2.0 48.1 1.0 ND E:HEM1001 2.0 47.2 1.0 NE2 E:HIS97 2.1 48.6 1.0 CE1 E:HIS198 2.8 46.9 1.0 C1A E:HEM1001 2.9 47.8 1.0 C4A E:HEM1001 3.0 48.2 1.0 HE1 E:HIS198 3.0 55.7 1.0 C4B E:HEM1001 3.0 48.3 1.0 C4C E:HEM1001 3.0 47.1 1.0 CE1 E:HIS97 3.0 48.9 1.0 C1C E:HEM1001 3.0 47.6 1.0 CD2 E:HIS198 3.0 46.3 1.0 C4D E:HEM1001 3.0 49.0 1.0 C1B E:HEM1001 3.1 48.5 1.0 C1D E:HEM1001 3.1 47.0 1.0 HE1 E:HIS97 3.2 58.1 1.0 CD2 E:HIS97 3.2 49.0 1.0 HD2 E:HIS198 3.3 55.0 1.0 CHA E:HEM1001 3.3 47.5 1.0 CHC E:HEM1001 3.4 48.1 1.0 CHB E:HEM1001 3.4 48.5 1.0 HD2 E:HIS97 3.4 58.2 1.0 CHD E:HEM1001 3.5 46.9 1.0 ND1 E:HIS198 4.0 46.4 1.0 CG E:HIS198 4.1 46.1 1.0 HA3 E:GLY146 4.1 62.0 1.0 C2A E:HEM1001 4.2 48.1 1.0 C3A E:HEM1001 4.2 49.0 1.0 ND1 E:HIS97 4.2 49.5 1.0 C3C E:HEM1001 4.2 48.1 1.0 C3B E:HEM1001 4.3 48.7 1.0 C2C E:HEM1001 4.3 47.3 1.0 CG E:HIS97 4.3 49.6 1.0 C3D E:HEM1001 4.3 47.0 1.0 HHA E:HEM1001 4.3 56.9 1.0 C2B E:HEM1001 4.3 48.9 1.0 C2D E:HEM1001 4.3 46.9 1.0 HHC E:HEM1001 4.3 57.4 1.0 HE21 E:GLN58 4.4 60.5 1.0 HHB E:HEM1001 4.4 57.9 1.0 HHD E:HEM1001 4.4 56.0 1.0 HA2 E:GLY146 4.6 62.0 1.0 HA3 E:GLY62 4.7 62.4 1.0 HA2 E:GLY62 4.7 62.4 1.0 HE22 E:GLN58 4.8 60.5 1.0 NE2 E:GLN58 4.8 50.4 1.0 CA E:GLY146 4.8 51.6 1.0 HD12 E:LEU149 4.9 54.3 1.0

Iron binding site 7 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe1002 b:59.1 occ:1.00 FE E:HEM1002 0.0 59.1 1.0 ND E:HEM1002 1.9 60.7 1.0 NC E:HEM1002 1.9 57.9 1.0 NE2 E:HIS212 2.1 58.6 1.0 NB E:HEM1002 2.1 57.7 1.0 NA E:HEM1002 2.1 60.4 1.0 NE2 E:HIS111 2.2 59.8 1.0 C1D E:HEM1002 2.9 60.6 1.0 C4C E:HEM1002 2.9 58.2 1.0 C1C E:HEM1002 3.0 56.8 1.0 CE1 E:HIS212 3.0 58.5 1.0 C4D E:HEM1002 3.0 62.1 1.0 C4B E:HEM1002 3.1 56.5 1.0 CD2 E:HIS212 3.1 58.2 1.0 CD2 E:HIS111 3.1 59.1 1.0 C1A E:HEM1002 3.1 61.9 1.0 C1B E:HEM1002 3.1 57.7 1.0 C4A E:HEM1002 3.2 60.0 1.0 HE1 E:HIS212 3.2 69.6 1.0 HD2 E:HIS111 3.2 70.3 1.0 CHD E:HEM1002 3.2 59.5 1.0 CE1 E:HIS111 3.2 61.0 1.0 HD2 E:HIS212 3.3 69.3 1.0 CHC E:HEM1002 3.4 56.1 1.0 CHA E:HEM1002 3.4 62.7 1.0 HE1 E:HIS111 3.4 72.6 1.0 CHB E:HEM1002 3.5 58.8 1.0 C2D E:HEM1002 4.1 62.0 1.0 ND1 E:HIS212 4.1 58.1 1.0 C3D E:HEM1002 4.2 63.0 1.0 HHD E:HEM1002 4.2 70.8 1.0 C3C E:HEM1002 4.2 57.2 1.0 CG E:HIS212 4.2 57.8 1.0 C2C E:HEM1002 4.2 56.3 1.0 CG E:HIS111 4.3 59.8 1.0 ND1 E:HIS111 4.3 61.0 1.0 C2A E:HEM1002 4.3 62.5 1.0 C3B E:HEM1002 4.3 55.8 1.0 C3A E:HEM1002 4.3 61.3 1.0 HHC E:HEM1002 4.4 66.8 1.0 C2B E:HEM1002 4.4 56.5 1.0 HHA E:HEM1002 4.4 74.6 1.0 HHB E:HEM1002 4.5 70.0 1.0 HD12 E:LEU51 4.7 68.2 1.0 HH22 E:ARG114 4.7 76.0 1.0 HA2 E:GLY48 4.8 72.7 1.0 HD13 E:LEU51 4.8 68.2 1.0 HG22 E:THR128 4.8 73.5 1.0 HE2 E:PHE216 5.0 89.0 1.0

Iron binding site 8 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1001 b:68.0 occ:1.00 FE F:HEC1001 0.0 68.0 1.0 NE2 F:HIS40 2.0 66.0 1.0 NC F:HEC1001 2.0 67.8 1.0 NA F:HEC1001 2.0 65.7 1.0 ND F:HEC1001 2.0 65.3 1.0 NB F:HEC1001 2.1 63.5 1.0 SD F:MET185 2.2 68.1 1.0 CE1 F:HIS40 3.0 66.8 1.0 CD2 F:HIS40 3.0 66.5 1.0 C4C F:HEC1001 3.0 69.5 1.0 C1A F:HEC1001 3.0 66.0 1.0 C1D F:HEC1001 3.0 67.0 1.0 C4D F:HEC1001 3.0 65.2 1.0 C4A F:HEC1001 3.1 63.9 1.0 C1C F:HEC1001 3.1 66.1 1.0 C1B F:HEC1001 3.1 63.0 1.0 C4B F:HEC1001 3.1 64.1 1.0 HE1 F:HIS40 3.2 80.3 1.0 HD2 F:HIS40 3.2 79.9 1.0 CHD F:HEC1001 3.4 69.2 1.0 CHA F:HEC1001 3.4 66.2 1.0 CG F:MET185 3.4 67.9 1.0 HG3 F:MET185 3.4 81.5 1.0 CHC F:HEC1001 3.5 65.1 1.0 CHB F:HEC1001 3.5 63.1 1.0 HB2 F:MET185 3.5 86.2 1.0 CE F:MET185 3.5 68.6 1.0 HE1 F:MET185 3.6 82.4 1.0 HE2 F:MET185 3.8 82.4 1.0 CB F:MET185 4.0 71.7 1.0 ND1 F:HIS40 4.1 64.5 1.0 CG F:HIS40 4.1 63.0 1.0 HG2 F:MET185 4.2 81.5 1.0 C2A F:HEC1001 4.2 63.4 1.0 C3C F:HEC1001 4.3 68.0 1.0 C3D F:HEC1001 4.3 65.2 1.0 C2D F:HEC1001 4.3 68.6 1.0 C3A F:HEC1001 4.3 62.6 1.0 C2C F:HEC1001 4.3 66.0 1.0 HE3 F:MET185 4.3 82.4 1.0 C2B F:HEC1001 4.3 63.5 1.0 C3B F:HEC1001 4.3 64.3 1.0 HHD F:HEC1001 4.3 83.2 1.0 HHA F:HEC1001 4.4 79.5 1.0 HHC F:HEC1001 4.5 78.2 1.0 HHB F:HEC1001 4.5 75.8 1.0 HB3 F:MET185 4.5 86.2 1.0 HD2 F:PRO98 4.6 71.3 1.0 HD21 F:LEU100 4.7 62.8 1.0 HB1 F:ALA97 4.8 80.6 1.0 HB2 F:CYS39 5.0 73.5 1.0 HG3 F:PRO188 5.0 74.5 1.0

Iron binding site 9 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe1001 b:65.4 occ:1.00 FE1 G:FES1001 0.0 65.4 1.0 S1 G:FES1001 2.2 59.6 1.0 S2 G:FES1001 2.2 63.9 1.0 SG G:CYS149 2.2 60.6 1.0 SG G:CYS129 2.3 59.2 1.0 HB3 G:CYS129 2.9 70.2 1.0 CB G:CYS129 3.0 59.0 1.0 FE2 G:FES1001 3.0 65.9 1.0 HB2 G:CYS129 3.1 70.2 1.0 HB3 G:CYS149 3.1 76.7 1.0 HB2 G:CYS134 3.1 66.6 1.0 CB G:CYS149 3.2 63.8 1.0 HB2 G:CYS151 3.2 66.2 1.0 HB3 G:HIS131 3.2 70.8 1.0 HB2 G:CYS149 3.5 76.7 1.0 H G:CYS134 3.9 65.7 1.0 HB2 G:SER154 3.9 74.8 1.0 H G:HIS152 3.9 91.7 1.0 H G:LEU132 3.9 64.3 1.0 CB G:CYS134 4.1 56.0 1.0 H G:CYS151 4.1 75.3 1.0 CB G:HIS131 4.1 58.9 1.0 CB G:CYS151 4.2 55.0 1.0 HB2 G:HIS131 4.2 70.8 1.0 H G:HIS131 4.3 74.4 1.0 CA G:CYS129 4.4 59.7 1.0 HB3 G:CYS151 4.5 66.2 1.0 HG G:SER154 4.5 73.4 1.0 N G:CYS134 4.5 55.2 1.0 HB3 G:CYS134 4.5 66.6 1.0 CA G:CYS149 4.5 67.3 1.0 H G:SER154 4.5 74.4 1.0 HH G:TYR156 4.6 85.3 1.0 N G:HIS152 4.6 76.3 1.0 H G:GLY133 4.6 64.5 1.0 ND1 G:HIS131 4.7 58.9 1.0 OG G:SER154 4.7 61.6 1.0 CB G:SER154 4.7 62.9 1.0 HB2 G:ALA167 4.8 79.6 1.0 N G:LEU132 4.8 54.0 1.0 CA G:CYS134 4.8 56.0 1.0 HA G:CYS129 4.8 71.1 1.0 N G:CYS151 4.8 62.7 1.0 HA G:CYS149 4.8 80.8 1.0 C G:CYS149 4.8 68.6 1.0 ND1 G:HIS152 4.8 65.0 1.0 HB2 G:HIS152 4.8 84.7 1.0 SG G:CYS134 4.9 54.2 1.0 CG G:HIS131 4.9 59.7 1.0 O G:CYS149 4.9 70.3 1.0 C G:CYS129 5.0 58.8 1.0 N G:HIS131 5.0 61.9 1.0 CA G:CYS151 5.0 58.9 1.0

Iron binding site 10 out of 20 in the Rhodobacter Sphaeroides BC1 with Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Rhodobacter Sphaeroides BC1 with Famoxadone within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe1001 b:65.9 occ:1.00 FE2 G:FES1001 0.0 65.9 1.0 ND1 G:HIS131 2.2 58.9 1.0 ND1 G:HIS152 2.2 65.0 1.0 S1 G:FES1001 2.2 59.6 1.0 S2 G:FES1001 2.2 63.9 1.0 HB3 G:HIS131 2.7 70.8 1.0 HB2 G:HIS152 2.8 84.7 1.0 FE1 G:FES1001 3.0 65.4 1.0 CG G:HIS131 3.1 59.7 1.0 CG G:HIS152 3.1 66.0 1.0 CE1 G:HIS152 3.2 63.4 1.0 CE1 G:HIS131 3.2 57.6 1.0 CB G:HIS131 3.3 58.9 1.0 HE1 G:HIS152 3.4 76.2 1.0 CB G:HIS152 3.4 70.5 1.0 HE1 G:HIS131 3.4 69.3 1.0 HB2 G:CYS151 3.5 66.2 1.0 H G:HIS152 3.5 91.7 1.0 H G:LEU132 3.5 64.3 1.0 HB2 G:LEU132 3.5 61.2 1.0 HB3 G:CYS151 3.7 66.2 1.0 HB2 G:HIS131 3.7 70.8 1.0 N G:HIS152 3.7 76.3 1.0 HD12 G:LEU132 3.9 59.8 1.0 CB G:CYS151 4.0 55.0 1.0 N G:LEU132 4.1 54.0 1.0 CA G:HIS152 4.1 75.9 1.0 HB3 G:HIS152 4.2 84.7 1.0 HG G:LEU132 4.2 60.8 1.0 CD2 G:HIS131 4.2 59.2 1.0 NE2 G:HIS131 4.3 58.0 1.0 NE2 G:HIS152 4.3 62.6 1.0 CD2 G:HIS152 4.3 64.0 1.0 C G:CYS151 4.3 64.6 1.0 CB G:LEU132 4.4 51.5 1.0 HG2 G:PRO166 4.4 69.2 1.0 SG G:CYS129 4.5 59.2 1.0 CA G:HIS131 4.6 59.4 1.0 CG G:LEU132 4.6 51.1 1.0 HB2 G:PRO166 4.7 68.8 1.0 CD1 G:LEU132 4.7 50.3 1.0 CA G:CYS151 4.8 58.9 1.0 HG G:SER154 4.8 73.4 1.0 C G:HIS131 4.8 57.0 1.0 CA G:LEU132 4.8 52.6 1.0 HB2 G:CYS134 4.8 66.6 1.0 SG G:CYS149 4.9 60.6 1.0 C G:HIS152 4.9 79.6 1.0 HA G:HIS152 4.9 91.2 1.0 HD2 G:PRO166 4.9 71.4 1.0

L.Esser, F.Zhou, Y.Zhou, Y.Xiao, W.K.Tang, C.A.Yu, Z.Qin, D.Xia. Hydrogen Bonding to the Substrate Is Not Required For Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III. J.Biol.Chem. V. 291 25019 2016.
ISSN: ESSN 1083-351X
PubMed: 27758861
DOI: 10.1074/JBC.M116.744391