Iron in PDB 7awt: E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm

The structure of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm also contains other interesting chemical elements:

Magnesium

(Mg)

8 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 32;

Binding sites:

The binding sites of Iron atom in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm (pdb code 7awt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm, PDB code: 7awt:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:115.2 occ:1.00 FE1 B:SF4301 0.0 115.2 1.0 SG B:CYS129 2.3 101.1 1.0 S3 B:SF4301 2.3 115.2 1.0 S4 B:SF4301 2.3 115.2 1.0 S2 B:SF4301 2.3 115.2 1.0 CB B:CYS129 2.7 101.1 1.0 FE2 B:SF4301 2.7 115.2 1.0 FE4 B:SF4301 2.7 115.2 1.0 FE3 B:SF4301 2.7 115.2 1.0 S1 B:SF4301 3.9 115.2 1.0 CA B:CYS129 3.9 101.1 1.0 N B:CYS129 3.9 101.1 1.0 OG1 B:THR101 4.5 108.1 1.0 SG B:CYS158 4.6 101.7 1.0 N B:THR101 4.7 108.1 1.0 SG B:CYS64 4.8 116.6 1.0 NH2 D:ARG250 4.9 98.6 1.0 O B:ALA99 5.0 113.6 1.0 SG B:CYS63 5.0 115.6 1.0 C B:ALA128 5.0 97.6 1.0

Iron binding site 2 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:115.2 occ:1.00 FE2 B:SF4301 0.0 115.2 1.0 SG B:CYS64 2.3 116.6 1.0 S4 B:SF4301 2.3 115.2 1.0 S3 B:SF4301 2.3 115.2 1.0 S1 B:SF4301 2.3 115.2 1.0 FE1 B:SF4301 2.7 115.2 1.0 FE4 B:SF4301 2.7 115.2 1.0 FE3 B:SF4301 2.7 115.2 1.0 CB B:CYS64 3.3 116.6 1.0 N B:CYS64 3.8 116.6 1.0 CA B:CYS64 3.9 116.6 1.0 S2 B:SF4301 3.9 115.2 1.0 O B:ALA99 4.1 113.6 1.0 CB B:PRO159 4.3 107.1 1.0 SG B:CYS63 4.4 115.6 1.0 CA B:PRO159 4.5 107.1 1.0 CB B:CYS129 4.7 101.1 1.0 CA B:GLY127 4.8 101.8 1.0 C B:CYS63 4.8 115.6 1.0 SG B:CYS158 4.9 101.7 1.0 CA B:CYS158 4.9 101.7 1.0 SG B:CYS129 4.9 101.1 1.0

Iron binding site 3 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:115.2 occ:1.00 FE3 B:SF4301 0.0 115.2 1.0 SG B:CYS63 2.3 115.6 1.0 S1 B:SF4301 2.3 115.2 1.0 S2 B:SF4301 2.3 115.2 1.0 S4 B:SF4301 2.3 115.2 1.0 FE2 B:SF4301 2.7 115.2 1.0 FE4 B:SF4301 2.7 115.2 1.0 FE1 B:SF4301 2.7 115.2 1.0 CB B:CYS63 3.9 115.6 1.0 S3 B:SF4301 3.9 115.2 1.0 N B:CYS63 4.1 115.6 1.0 N B:CYS64 4.1 116.6 1.0 CB B:SER62 4.2 116.6 1.0 NE2 D:HIS355 4.2 97.8 1.0 NH2 D:ARG250 4.3 98.6 1.0 CA B:CYS63 4.4 115.6 1.0 C B:CYS63 4.6 115.6 1.0 SG B:CYS158 4.7 101.7 1.0 CG D:ARG270 4.7 90.8 1.0 SG B:CYS129 4.7 101.1 1.0 SG B:CYS64 4.8 116.6 1.0 C B:SER62 4.9 116.6 1.0 CD2 D:HIS355 4.9 97.8 1.0

Iron binding site 4 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:115.2 occ:1.00 FE4 B:SF4301 0.0 115.2 1.0 SG B:CYS158 2.3 101.7 1.0 S2 B:SF4301 2.3 115.2 1.0 S1 B:SF4301 2.3 115.2 1.0 S3 B:SF4301 2.3 115.2 1.0 FE2 B:SF4301 2.7 115.2 1.0 FE1 B:SF4301 2.7 115.2 1.0 FE3 B:SF4301 2.7 115.2 1.0 CB B:CYS158 3.3 101.7 1.0 CA B:CYS158 3.5 101.7 1.0 S4 B:SF4301 3.9 115.2 1.0 C B:CYS158 3.9 101.7 1.0 N B:PRO159 4.3 107.1 1.0 O B:CYS158 4.4 101.7 1.0 SG B:CYS129 4.5 101.1 1.0 SG B:CYS63 4.5 115.6 1.0 NE D:ARG270 4.6 90.8 1.0 NH2 D:ARG270 4.6 90.8 1.0 CA B:PRO159 4.6 107.1 1.0 CE B:MET135 4.7 88.2 1.0 SG B:CYS64 4.7 116.6 1.0 CD2 D:HIS355 4.8 97.8 1.0 N B:CYS158 4.9 101.7 1.0 NE2 D:HIS355 4.9 97.8 1.0 O B:GLY157 4.9 102.2 1.0 CB B:PRO159 5.0 107.1 1.0

Iron binding site 5 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:98.3 occ:1.00 FE1 E:FES201 0.0 98.3 1.0 S1 E:FES201 2.2 98.3 1.0 S2 E:FES201 2.2 98.3 1.0 SG E:CYS92 2.2 89.3 1.0 SG E:CYS97 2.3 87.0 1.0 FE2 E:FES201 2.7 98.3 1.0 CB E:CYS97 3.2 87.0 1.0 CB E:CYS92 3.2 89.3 1.0 N E:CYS97 4.0 87.0 1.0 CA E:CYS97 4.1 87.0 1.0 SG E:CYS133 4.2 90.8 1.0 N E:LEU134 4.5 87.8 1.0 CA E:CYS92 4.5 89.3 1.0 C E:CYS92 4.5 89.3 1.0 O E:CYS92 4.6 89.3 1.0 CA E:CYS133 4.6 90.8 1.0 SG E:CYS137 4.7 87.8 1.0 N E:SER94 4.7 85.4 1.0 ND2 E:ASN142 4.9 88.6 1.0 CB E:SER94 4.9 85.4 1.0 N E:ASN142 4.9 88.6 1.0 CB E:CYS133 4.9 90.8 1.0 C E:VAL96 5.0 85.5 1.0

Iron binding site 6 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:98.3 occ:1.00 FE2 E:FES201 0.0 98.3 1.0 S2 E:FES201 2.2 98.3 1.0 S1 E:FES201 2.2 98.3 1.0 SG E:CYS133 2.2 90.8 1.0 SG E:CYS137 2.3 87.8 1.0 FE1 E:FES201 2.7 98.3 1.0 CB E:CYS137 3.5 87.8 1.0 CB E:CYS133 3.8 90.8 1.0 CA E:CYS137 3.8 87.8 1.0 N E:CYS137 3.9 87.8 1.0 SG E:CYS92 4.0 89.3 1.0 N E:LEU134 4.2 87.8 1.0 N E:GLY135 4.3 88.5 1.0 CA E:CYS133 4.3 90.8 1.0 SG E:CYS97 4.4 87.0 1.0 N E:ASN136 4.5 86.9 1.0 CB E:VAL96 4.5 85.5 1.0 C E:ASN136 4.7 86.9 1.0 C E:CYS133 4.7 90.8 1.0 CA E:GLY135 4.8 88.5 1.0 N F:GLY97 4.8 88.0 1.0 CG2 E:VAL96 4.8 85.5 1.0

Iron binding site 7 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:85.0 occ:1.00 FE1 F:SF4501 0.0 85.0 1.0 S2 F:SF4501 2.3 85.0 1.0 SG F:CYS351 2.3 81.2 1.0 S3 F:SF4501 2.3 85.0 1.0 S4 F:SF4501 2.3 85.0 1.0 FE3 F:SF4501 2.7 85.0 1.0 FE4 F:SF4501 2.7 85.0 1.0 FE2 F:SF4501 2.7 85.0 1.0 CB F:CYS351 3.7 81.2 1.0 S1 F:SF4501 3.9 85.0 1.0 N F:CYS351 3.9 81.2 1.0 CA F:CYS351 4.1 81.2 1.0 O F:CYS351 4.1 81.2 1.0 C F:CYS351 4.1 81.2 1.0 N F:TRP353 4.2 74.7 1.0 CB F:TRP353 4.4 74.7 1.0 N F:CYS354 4.5 77.2 1.0 CD F:PRO197 4.6 78.5 1.0 CA F:TRP353 4.7 74.7 1.0 SG F:CYS398 4.7 77.7 1.0 N F:GLY352 4.8 77.6 1.0 SG F:CYS357 4.8 78.3 1.0 SG F:CYS354 4.8 77.2 1.0 CG F:PRO197 4.9 78.5 1.0 CD1 F:ILE179 4.9 80.0 1.0

Iron binding site 8 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:85.0 occ:1.00 FE2 F:SF4501 0.0 85.0 1.0 S3 F:SF4501 2.3 85.0 1.0 S1 F:SF4501 2.3 85.0 1.0 SG F:CYS357 2.3 78.3 1.0 S4 F:SF4501 2.3 85.0 1.0 FE4 F:SF4501 2.7 85.0 1.0 FE1 F:SF4501 2.7 85.0 1.0 FE3 F:SF4501 2.7 85.0 1.0 CB F:CYS357 2.8 78.3 1.0 CD2 F:HIS400 3.6 79.8 1.0 S2 F:SF4501 3.9 85.0 1.0 CB F:SER350 4.0 80.5 1.0 CG F:HIS400 4.2 79.8 1.0 CA F:CYS357 4.2 78.3 1.0 SG F:CYS354 4.2 77.2 1.0 CB F:HIS400 4.3 79.8 1.0 N F:CYS351 4.5 81.2 1.0 NE2 F:HIS400 4.6 79.8 1.0 N F:ARG358 4.7 76.0 1.0 O F:CYS351 4.7 81.2 1.0 SG F:CYS398 4.7 77.7 1.0 C F:CYS357 4.7 78.3 1.0 SG F:CYS351 4.7 81.2 1.0 N F:ALA401 4.8 79.0 1.0 CA F:SER350 4.8 80.5 1.0 CB F:ALA401 4.9 79.0 1.0 OG F:SER350 4.9 80.5 1.0

Iron binding site 9 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:85.0 occ:1.00 FE3 F:SF4501 0.0 85.0 1.0 SG F:CYS398 2.2 77.7 1.0 S4 F:SF4501 2.3 85.0 1.0 S2 F:SF4501 2.3 85.0 1.0 S1 F:SF4501 2.3 85.0 1.0 FE1 F:SF4501 2.7 85.0 1.0 FE4 F:SF4501 2.7 85.0 1.0 FE2 F:SF4501 2.7 85.0 1.0 CB F:CYS398 3.3 77.7 1.0 CB F:HIS400 3.7 79.8 1.0 S3 F:SF4501 3.9 85.0 1.0 N F:CYS398 3.9 77.7 1.0 CA F:CYS398 4.0 77.7 1.0 N F:HIS400 4.3 79.8 1.0 C F:CYS398 4.3 77.7 1.0 CD1 F:ILE179 4.5 80.0 1.0 CG F:PRO197 4.5 78.5 1.0 CG F:HIS400 4.5 79.8 1.0 CA F:HIS400 4.6 79.8 1.0 O F:CYS398 4.6 77.7 1.0 SG F:CYS351 4.7 81.2 1.0 CD2 F:HIS400 4.7 79.8 1.0 SG F:CYS354 4.8 77.2 1.0 SG F:CYS357 4.8 78.3 1.0 N F:ALA401 4.9 79.0 1.0 N F:ALA399 4.9 79.1 1.0 C F:PHE397 4.9 75.3 1.0 CB F:CYS357 4.9 78.3 1.0

Iron binding site 10 out of 32 in the E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of E. Coli Nadh Quinone Oxidoreductase Hydrophilic Arm within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:85.0 occ:1.00 FE4 F:SF4501 0.0 85.0 1.0 SG F:CYS354 2.3 77.2 1.0 S1 F:SF4501 2.3 85.0 1.0 S2 F:SF4501 2.3 85.0 1.0 S3 F:SF4501 2.3 85.0 1.0 FE2 F:SF4501 2.7 85.0 1.0 FE1 F:SF4501 2.7 85.0 1.0 FE3 F:SF4501 2.7 85.0 1.0 CB F:CYS354 3.1 77.2 1.0 N F:CYS354 3.6 77.2 1.0 CB F:CYS357 3.8 78.3 1.0 CA F:CYS354 3.8 77.2 1.0 S4 F:SF4501 3.9 85.0 1.0 O F:CYS354 4.1 77.2 1.0 CB F:PHE397 4.2 75.3 1.0 N F:PHE397 4.3 75.3 1.0 C F:CYS354 4.4 77.2 1.0 SG F:CYS357 4.5 78.3 1.0 N F:CYS398 4.5 77.7 1.0 C F:TRP353 4.7 74.7 1.0 CA F:PHE397 4.7 75.3 1.0 SG F:CYS398 4.8 77.7 1.0 CB F:THR396 4.8 78.6 1.0 SG F:CYS351 4.8 81.2 1.0 CB F:TRP353 4.9 74.7 1.0

J.Schimpf, S.Oppermann, T.Gerasimova, A.F.Santos Seica, P.Hellwig, I.Grishkovskaya, D.Haselbach, T.Friedrich. Structure of the Peripheral Arm of A Minimalistic Respiratory Complex I To Be Published.