Iron in PDB 7ar7: Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)

All present enzymatic activity of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation):
7.1.1.2;

The structure of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Iron atom in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) (pdb code 7ar7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation), PDB code: 7ar7:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:50.3 occ:1.00 FE1 B:SF4500 0.0 50.3 1.0 SG B:CYS158 2.3 50.3 1.0 S3 B:SF4500 2.3 50.3 1.0 S4 B:SF4500 2.3 50.3 1.0 S2 B:SF4500 2.3 50.3 1.0 CB B:CYS158 2.7 50.3 1.0 FE4 B:SF4500 2.7 50.3 1.0 FE3 B:SF4500 2.7 50.3 1.0 FE2 B:SF4500 2.7 50.3 1.0 N B:CYS158 3.4 50.3 1.0 CA B:CYS158 3.6 50.3 1.0 S1 B:SF4500 3.9 50.3 1.0 OG1 B:THR130 4.1 33.4 1.0 C B:SER157 4.5 39.4 1.0 SG B:CYS188 4.7 50.3 1.0 N B:SER157 4.7 39.4 1.0 SG B:CYS94 4.8 36.0 1.0 C B:CYS158 4.9 50.3 1.0 N B:THR130 4.9 33.4 1.0 SG B:CYS93 4.9 30.3 1.0 CA B:SER157 5.0 39.4 1.0

Iron binding site 2 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:50.3 occ:1.00 FE2 B:SF4500 0.0 50.3 1.0 SG B:CYS94 2.3 36.0 1.0 S4 B:SF4500 2.3 50.3 1.0 S1 B:SF4500 2.3 50.3 1.0 S3 B:SF4500 2.3 50.3 1.0 FE4 B:SF4500 2.7 50.3 1.0 FE3 B:SF4500 2.7 50.3 1.0 FE1 B:SF4500 2.7 50.3 1.0 CB B:CYS94 3.5 36.0 1.0 S2 B:SF4500 3.9 50.3 1.0 N B:CYS94 3.9 36.0 1.0 SG B:CYS93 3.9 30.3 1.0 CA B:CYS94 4.1 36.0 1.0 CA B:GLY156 4.4 50.3 1.0 CB B:PRO189 4.5 36.5 1.0 N B:SER157 4.5 39.4 1.0 CA B:PRO189 4.5 36.5 1.0 O B:GLY187 4.7 42.4 1.0 C B:CYS93 4.8 30.3 1.0 CA B:CYS188 4.8 50.3 1.0 N B:CYS158 4.8 50.3 1.0 CB B:CYS158 4.9 50.3 1.0 SG B:CYS188 4.9 50.3 1.0 C B:GLY156 4.9 50.3 1.0 CA B:GLY129 4.9 50.3 1.0 SG B:CYS158 5.0 50.3 1.0

Iron binding site 3 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:50.3 occ:1.00 FE3 B:SF4500 0.0 50.3 1.0 SG B:CYS188 2.3 50.3 1.0 S1 B:SF4500 2.3 50.3 1.0 S2 B:SF4500 2.3 50.3 1.0 S4 B:SF4500 2.3 50.3 1.0 FE1 B:SF4500 2.7 50.3 1.0 FE4 B:SF4500 2.7 50.3 1.0 FE2 B:SF4500 2.7 50.3 1.0 CB B:CYS188 3.2 50.3 1.0 CA B:CYS188 3.5 50.3 1.0 S3 B:SF4500 3.9 50.3 1.0 C B:CYS188 4.0 50.3 1.0 SG B:CYS93 4.2 30.3 1.0 NE D:ARG69 4.3 50.3 1.0 N B:PRO189 4.4 36.5 1.0 NH2 D:ARG69 4.5 50.3 1.0 O B:CYS188 4.5 50.3 1.0 CD2 D:HIS154 4.5 50.3 1.0 SG B:CYS158 4.6 50.3 1.0 CA B:PRO189 4.7 36.5 1.0 SG B:CYS94 4.7 36.0 1.0 O B:GLY187 4.7 42.4 1.0 NE2 D:HIS154 4.7 50.3 1.0 N B:CYS188 4.8 50.3 1.0 CZ D:ARG69 4.9 50.3 1.0 CB B:SER157 4.9 39.4 1.0 N B:SER157 4.9 39.4 1.0

Iron binding site 4 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:50.3 occ:1.00 FE4 B:SF4500 0.0 50.3 1.0 SG B:CYS93 2.2 30.3 1.0 S2 B:SF4500 2.3 50.3 1.0 S3 B:SF4500 2.3 50.3 1.0 S1 B:SF4500 2.3 50.3 1.0 FE1 B:SF4500 2.7 50.3 1.0 FE2 B:SF4500 2.7 50.3 1.0 FE3 B:SF4500 2.7 50.3 1.0 S4 B:SF4500 3.9 50.3 1.0 CB B:CYS93 3.9 30.3 1.0 CG D:ARG69 4.2 50.3 1.0 NE2 D:HIS154 4.2 50.3 1.0 N B:CYS93 4.3 30.3 1.0 SG B:CYS158 4.5 50.3 1.0 N B:CYS94 4.5 36.0 1.0 CA B:CYS93 4.6 30.3 1.0 SG B:CYS188 4.7 50.3 1.0 CB B:ALA92 4.7 27.3 1.0 SG B:CYS94 4.8 36.0 1.0 CD2 D:HIS154 4.8 50.3 1.0 C B:CYS93 4.9 30.3 1.0 NE D:ARG69 4.9 50.3 1.0 NH1 D:ARG49 4.9 50.3 1.0

Iron binding site 5 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe500 b:139.7 occ:1.00 FE1 E:FES500 0.0 139.7 1.0 S2 E:FES500 2.2 139.7 1.0 S1 E:FES500 2.2 139.7 1.0 SG E:CYS135 2.3 116.7 1.0 FE2 E:FES500 2.7 139.7 1.0 CB E:CYS135 2.8 116.7 1.0 SG E:CYS171 2.9 108.2 1.0 N E:GLY131 3.2 90.1 1.0 OG E:SER140 3.4 117.0 1.0 CA E:GLY131 3.6 90.1 1.0 CE E:MET169 3.7 86.0 1.0 CE E:MET180 3.8 95.0 1.0 O E:ALA178 3.9 103.4 1.0 C E:GLY131 4.2 90.1 1.0 CA E:CYS135 4.3 116.7 1.0 C E:CYS130 4.3 90.7 1.0 CB E:SER140 4.5 117.0 1.0 CB E:CYS175 4.5 115.4 1.0 N E:THR132 4.5 99.5 1.0 CA E:CYS130 4.6 90.7 1.0 SG E:CYS175 4.7 115.4 1.0 CB E:CYS171 4.7 108.2 1.0 O E:GLY131 4.8 90.1 1.0 O E:THR132 4.9 99.5 1.0 CB E:CYS130 5.0 90.7 1.0

Iron binding site 6 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe500 b:139.7 occ:1.00 FE2 E:FES500 0.0 139.7 1.0 CB E:CYS175 1.9 115.4 1.0 S1 E:FES500 2.2 139.7 1.0 S2 E:FES500 2.2 139.7 1.0 SG E:CYS171 2.3 108.2 1.0 SG E:CYS175 2.3 115.4 1.0 FE1 E:FES500 2.7 139.7 1.0 CB E:CYS135 2.9 116.7 1.0 CE E:MET180 3.1 95.0 1.0 SG E:CYS135 3.3 116.7 1.0 CA E:CYS175 3.4 115.4 1.0 CB E:CYS171 3.6 108.2 1.0 CA E:CYS135 4.0 116.7 1.0 O E:CYS175 4.1 115.4 1.0 C E:CYS175 4.2 115.4 1.0 N E:CYS175 4.2 115.4 1.0 N E:CYS135 4.4 116.7 1.0 CA E:CYS171 4.7 108.2 1.0 SD E:MET180 4.8 95.0 1.0 O E:GLY173 4.9 89.1 1.0 O E:ASN177 5.0 100.3 1.0

Iron binding site 7 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:50.3 occ:1.00 FE1 F:SF4501 0.0 50.3 1.0 SG F:CYS405 2.3 39.0 1.0 S4 F:SF4501 2.3 50.3 1.0 S3 F:SF4501 2.3 50.3 1.0 S2 F:SF4501 2.3 50.3 1.0 FE2 F:SF4501 2.7 50.3 1.0 FE4 F:SF4501 2.7 50.3 1.0 FE3 F:SF4501 2.7 50.3 1.0 CB F:CYS405 3.6 39.0 1.0 N F:CYS405 3.6 39.0 1.0 CB F:CYS408 3.9 39.4 1.0 S1 F:SF4501 3.9 50.3 1.0 CA F:CYS405 4.1 39.0 1.0 CB F:ILE447 4.1 50.3 1.0 N F:ILE447 4.2 50.3 1.0 CB F:GLN404 4.4 50.3 1.0 O F:CYS405 4.5 39.0 1.0 SG F:CYS408 4.5 39.4 1.0 N F:GLN404 4.6 50.3 1.0 C F:GLN404 4.6 50.3 1.0 OE1 F:GLN404 4.6 50.3 1.0 CG1 F:ILE447 4.7 50.3 1.0 N F:CYS448 4.7 37.9 1.0 C F:CYS405 4.7 39.0 1.0 CA F:ILE447 4.7 50.3 1.0 CA F:GLN404 4.8 50.3 1.0 CB F:THR446 4.8 35.3 1.0 SG F:CYS448 4.9 37.9 1.0 O F:SER401 4.9 29.0 1.0 SG F:CYS402 4.9 26.4 1.0

Iron binding site 8 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:50.3 occ:1.00 FE2 F:SF4501 0.0 50.3 1.0 SG F:CYS408 2.3 39.4 1.0 S3 F:SF4501 2.3 50.3 1.0 S4 F:SF4501 2.3 50.3 1.0 S1 F:SF4501 2.3 50.3 1.0 CB F:CYS408 2.7 39.4 1.0 FE1 F:SF4501 2.7 50.3 1.0 FE3 F:SF4501 2.7 50.3 1.0 FE4 F:SF4501 2.7 50.3 1.0 O F:SER401 3.3 29.0 1.0 S2 F:SF4501 3.9 50.3 1.0 CA F:CYS408 4.2 39.4 1.0 C F:SER401 4.3 29.0 1.0 SG F:CYS405 4.3 39.0 1.0 CD2 F:LEU450 4.3 28.0 1.0 CB F:SER401 4.4 29.0 1.0 CB F:LEU450 4.5 28.0 1.0 CA F:SER401 4.6 29.0 1.0 C F:CYS408 4.6 39.4 1.0 SG F:CYS402 4.6 26.4 1.0 SG F:CYS448 4.7 37.9 1.0 N F:GLY451 4.8 29.9 1.0 CG F:LEU450 5.0 28.0 1.0

Iron binding site 9 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:50.3 occ:1.00 FE3 F:SF4501 0.0 50.3 1.0 SG F:CYS402 2.3 26.4 1.0 S2 F:SF4501 2.3 50.3 1.0 S1 F:SF4501 2.3 50.3 1.0 S4 F:SF4501 2.3 50.3 1.0 FE4 F:SF4501 2.7 50.3 1.0 FE2 F:SF4501 2.7 50.3 1.0 FE1 F:SF4501 2.7 50.3 1.0 O F:SER401 2.9 29.0 1.0 S3 F:SF4501 3.9 50.3 1.0 CB F:CYS402 3.9 26.4 1.0 N F:GLN404 4.0 50.3 1.0 C F:SER401 4.0 29.0 1.0 CB F:GLN404 4.0 50.3 1.0 CD F:PRO246 4.3 28.4 1.0 C F:CYS402 4.4 26.4 1.0 N F:GLY403 4.4 33.0 1.0 CA F:CYS402 4.5 26.4 1.0 OE1 F:GLN404 4.6 50.3 1.0 CA F:GLN404 4.6 50.3 1.0 SG F:CYS448 4.7 37.9 1.0 N F:CYS402 4.7 26.4 1.0 CG F:PRO246 4.8 28.4 1.0 O F:CYS402 4.8 26.4 1.0 CG1 F:ILE228 4.8 28.1 1.0 N F:CYS405 4.8 39.0 1.0 SG F:CYS408 4.8 39.4 1.0 CD1 F:ILE228 4.9 28.1 1.0 SG F:CYS405 4.9 39.0 1.0 C F:GLY403 5.0 33.0 1.0

Iron binding site 10 out of 28 in the Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryo-Em Structure of Arabidopsis Thaliana Complex-I (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe501 b:50.3 occ:1.00 FE4 F:SF4501 0.0 50.3 1.0 SG F:CYS448 2.3 37.9 1.0 S1 F:SF4501 2.3 50.3 1.0 S3 F:SF4501 2.3 50.3 1.0 S2 F:SF4501 2.3 50.3 1.0 FE3 F:SF4501 2.7 50.3 1.0 FE1 F:SF4501 2.7 50.3 1.0 FE2 F:SF4501 2.7 50.3 1.0 CB F:CYS448 3.4 37.9 1.0 N F:CYS448 3.7 37.9 1.0 S4 F:SF4501 3.9 50.3 1.0 CA F:CYS448 4.0 37.9 1.0 CB F:LEU450 4.2 28.0 1.0 C F:CYS448 4.4 37.9 1.0 CG F:PRO246 4.4 28.4 1.0 O F:CYS448 4.5 37.9 1.0 CD1 F:ILE228 4.6 28.1 1.0 N F:LEU450 4.6 28.0 1.0 SG F:CYS402 4.7 26.4 1.0 SG F:CYS405 4.7 39.0 1.0 SG F:CYS408 4.8 39.4 1.0 CD F:PRO246 4.8 28.4 1.0 CB F:ILE447 4.8 50.3 1.0 C F:ILE447 4.9 50.3 1.0 O F:SER401 4.9 29.0 1.0 N F:GLY451 4.9 29.9 1.0 N F:ILE447 4.9 50.3 1.0 CA F:LEU450 4.9 28.0 1.0 CB F:CYS408 5.0 39.4 1.0

N.Klusch, J.Senkler, O.Yildiz, W.Kuehlbrandt, H.P.Braun. A Ferredoxin Bridge Connects the Two Arms of Plant Mitochondrial Complex I. Plant Cell V. 33 2072 2021.
ISSN: ESSN 1532-298X
PubMed: 33768254
DOI: 10.1093/PLCELL/KOAB092