Iron in PDB 8rbq: Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced

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

Binding sites:

The binding sites of Iron atom in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced (pdb code 8rbq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced, PDB code: 8rbq:
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 Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:29.1 occ:1.00 FE1 A:FES200 0.0 29.1 1.0 SG A:CYS25 2.2 45.4 1.0 S1 A:FES200 2.2 34.9 1.0 S2 A:FES200 2.2 51.6 1.0 SG E:CYS122 2.2 75.0 1.0 FE2 A:FES200 2.8 47.5 1.0 CB A:CYS25 3.0 25.2 1.0 CB E:CYS122 3.4 69.2 1.0 CA A:CYS25 3.9 21.5 1.0 N A:CYS25 3.9 22.1 1.0 N E:CYS122 4.0 58.5 1.0 SG A:CYS113 4.1 51.5 1.0 N E:ALA37 4.2 40.8 1.0 CA E:CYS122 4.4 65.2 1.0 CD A:PRO26 4.6 31.0 1.0 O E:THR120 4.6 84.6 1.0 CA E:ALA37 4.6 33.7 1.0 SG E:CYS39 4.7 71.8 1.0 N E:LEU38 4.9 42.1 1.0 N A:PRO26 4.9 28.8 1.0 C A:CYS25 4.9 25.2 1.0

Iron binding site 2 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:47.5 occ:1.00 FE2 A:FES200 0.0 47.5 1.0 S1 A:FES200 2.2 34.9 1.0 S2 A:FES200 2.2 51.6 1.0 SG E:CYS39 2.3 71.8 1.0 SG A:CYS113 2.3 51.5 1.0 FE1 A:FES200 2.8 29.1 1.0 CB E:CYS39 3.3 48.2 1.0 CB A:CYS113 3.3 37.8 1.0 N E:CYS39 4.2 41.0 1.0 SG E:CYS122 4.3 75.0 1.0 CA E:CYS39 4.3 38.8 1.0 SG A:CYS25 4.4 45.4 1.0 O E:THR120 4.5 84.6 1.0 O A:ASN112 4.7 45.4 1.0 CA A:CYS113 4.7 29.4 1.0 N A:CYS25 4.7 22.1 1.0 N A:GLY23 4.8 14.4 1.0 N A:LEU24 4.8 20.3 1.0 C A:ASN112 4.9 44.2 1.0 N A:CYS113 4.9 33.1 1.0

Iron binding site 3 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:13.3 occ:1.00 FE1 C:SF4501 0.0 13.3 1.0 SG C:CYS376 2.3 33.8 1.0 S3 C:SF4501 2.3 11.4 1.0 S4 C:SF4501 2.3 22.7 1.0 S2 C:SF4501 2.3 31.2 1.0 FE2 C:SF4501 2.7 22.8 1.0 FE3 C:SF4501 2.7 21.6 1.0 FE4 C:SF4501 2.7 5.7 1.0 CB C:CYS376 3.5 3.9 1.0 S1 C:SF4501 3.9 13.7 1.0 N C:CYS376 4.1 11.0 1.0 SG C:CYS419 4.3 10.8 1.0 CB C:LEU387 4.3 14.6 1.0 CA C:CYS376 4.4 4.8 1.0 CD2 C:LEU387 4.5 4.2 1.0 SG C:CYS370 4.8 10.2 1.0 SG C:CYS373 4.8 21.6 1.0 N C:SER375 4.9 6.6 1.0 CD1 C:LEU425 4.9 4.6 1.0 CG C:LEU387 5.0 7.6 1.0 CA C:LEU387 5.0 10.0 1.0

Iron binding site 4 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:22.8 occ:1.00 FE2 C:SF4501 0.0 22.8 1.0 SG C:CYS419 2.3 10.8 1.0 S3 C:SF4501 2.3 11.4 1.0 S4 C:SF4501 2.3 22.7 1.0 S1 C:SF4501 2.3 13.7 1.0 FE1 C:SF4501 2.7 13.3 1.0 FE3 C:SF4501 2.7 21.6 1.0 FE4 C:SF4501 2.7 5.7 1.0 CB C:CYS419 3.8 0.0 1.0 OG C:SER421 3.9 4.3 1.0 S2 C:SF4501 3.9 31.2 1.0 SG C:CYS376 4.0 33.8 1.0 O C:SER421 4.1 21.1 1.0 CA C:CYS419 4.2 1.8 1.0 CD C:PRO420 4.4 8.9 1.0 SG C:CYS370 4.7 10.2 1.0 SG C:CYS373 4.7 21.6 1.0 N C:PRO420 4.7 4.4 1.0 CD1 C:LEU425 4.7 4.6 1.0 C C:CYS419 4.8 7.8 1.0 CD1 C:ILE423 4.8 8.5 1.0 N C:SER421 4.9 3.2 1.0

Iron binding site 5 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:21.6 occ:1.00 FE3 C:SF4501 0.0 21.6 1.0 SG C:CYS370 2.3 10.2 1.0 S4 C:SF4501 2.3 22.7 1.0 S1 C:SF4501 2.3 13.7 1.0 S2 C:SF4501 2.3 31.2 1.0 FE1 C:SF4501 2.7 13.3 1.0 FE2 C:SF4501 2.7 22.8 1.0 FE4 C:SF4501 2.7 5.7 1.0 CB C:CYS370 3.4 3.8 1.0 N C:ARG372 3.7 3.0 1.0 S3 C:SF4501 3.9 11.4 1.0 CA C:CYS370 4.0 1.1 1.0 CA C:ARG372 4.1 1.3 1.0 N C:ILE371 4.1 0.0 1.0 C C:CYS370 4.3 6.1 1.0 N C:CYS373 4.5 7.6 1.0 CB C:LEU387 4.5 14.6 1.0 SG C:CYS373 4.8 21.6 1.0 C C:ILE371 4.8 3.4 1.0 C C:ARG372 4.8 5.5 1.0 OG C:SER421 4.8 4.3 1.0 SG C:CYS419 4.9 10.8 1.0 SG C:CYS376 4.9 33.8 1.0

Iron binding site 6 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:5.7 occ:1.00 FE4 C:SF4501 0.0 5.7 1.0 SG C:CYS373 2.3 21.6 1.0 S3 C:SF4501 2.3 11.4 1.0 S1 C:SF4501 2.3 13.7 1.0 S2 C:SF4501 2.3 31.2 1.0 FE3 C:SF4501 2.7 21.6 1.0 FE2 C:SF4501 2.7 22.8 1.0 FE1 C:SF4501 2.7 13.3 1.0 N C:CYS373 3.5 7.6 1.0 CB C:CYS373 3.7 4.3 1.0 S4 C:SF4501 3.9 22.7 1.0 N C:ALA374 4.0 0.0 1.0 CA C:CYS373 4.0 4.8 1.0 CD C:PRO420 4.1 8.9 1.0 N C:SER375 4.2 6.6 1.0 C C:CYS373 4.3 10.4 1.0 SG C:CYS376 4.4 33.8 1.0 N C:ARG372 4.5 3.0 1.0 C C:ARG372 4.5 5.5 1.0 SG C:CYS419 4.6 10.8 1.0 CA C:ARG372 4.7 1.3 1.0 CG C:PRO420 4.8 0.8 1.0 CB C:SER375 4.8 6.7 1.0 SG C:CYS370 4.8 10.2 1.0 CG1 C:ILE371 4.8 1.0 1.0 CA C:ALA374 4.8 0.0 1.0 N C:CYS376 5.0 11.0 1.0

Iron binding site 7 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:30.9 occ:1.00 FE1 C:SF4502 0.0 30.9 1.0 SG C:CYS409 2.3 8.3 1.0 S2 C:SF4502 2.3 37.7 1.0 S4 C:SF4502 2.3 17.9 1.0 S3 C:SF4502 2.3 15.7 1.0 FE3 C:SF4502 2.7 19.2 1.0 FE2 C:SF4502 2.7 8.6 1.0 FE4 C:SF4502 2.7 21.5 1.0 CB C:CYS409 3.4 6.2 1.0 CA C:CYS409 3.6 3.6 1.0 S1 C:SF4502 3.9 15.1 1.0 N C:ILE410 3.9 3.2 1.0 N C:LEU411 4.1 15.7 1.0 C C:CYS409 4.2 13.7 1.0 CD1 C:LEU384 4.5 0.6 1.0 CD2 C:PHE429 4.7 10.1 1.0 CA C:LEU411 4.7 6.2 1.0 CE2 C:PHE429 4.8 8.9 1.0 N C:CYS412 4.8 3.0 1.0 SG C:CYS380 4.8 26.6 1.0 N C:CYS409 4.9 4.4 1.0 SG C:CYS415 4.9 27.2 1.0 SG C:CYS412 4.9 13.6 1.0 CA C:ILE410 5.0 0.6 1.0 C C:ILE410 5.0 10.2 1.0

Iron binding site 8 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:8.6 occ:1.00 FE2 C:SF4502 0.0 8.6 1.0 SG C:CYS412 2.3 13.6 1.0 S1 C:SF4502 2.3 15.1 1.0 S3 C:SF4502 2.3 15.7 1.0 S4 C:SF4502 2.3 17.9 1.0 FE3 C:SF4502 2.7 19.2 1.0 FE4 C:SF4502 2.7 21.5 1.0 FE1 C:SF4502 2.7 30.9 1.0 N C:CYS412 3.5 3.0 1.0 CB C:CYS412 3.5 8.4 1.0 S2 C:SF4502 3.9 37.7 1.0 CA C:CYS412 4.0 8.3 1.0 N C:GLY413 4.1 6.7 1.0 CD C:PRO381 4.2 14.3 1.0 C C:CYS412 4.4 7.8 1.0 N C:CYS414 4.5 12.6 1.0 N C:LEU411 4.5 15.7 1.0 C C:LEU411 4.5 4.1 1.0 CG1 C:ILE410 4.5 5.3 1.0 SG C:CYS415 4.6 27.2 1.0 SG C:CYS409 4.6 8.3 1.0 CA C:LEU411 4.8 6.2 1.0 SG C:CYS380 4.8 26.6 1.0 CB C:CYS414 4.9 4.6 1.0 N C:ILE410 5.0 3.2 1.0

Iron binding site 9 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:19.2 occ:1.00 FE3 C:SF4502 0.0 19.2 1.0 SG C:CYS415 2.2 27.2 1.0 S4 C:SF4502 2.3 17.9 1.0 S1 C:SF4502 2.3 15.1 1.0 S2 C:SF4502 2.3 37.7 1.0 FE1 C:SF4502 2.7 30.9 1.0 FE4 C:SF4502 2.7 21.5 1.0 FE2 C:SF4502 2.7 8.6 1.0 CE2 C:PHE429 3.7 8.9 1.0 CB C:CYS415 3.8 10.1 1.0 S3 C:SF4502 3.9 15.7 1.0 CD2 C:PHE429 4.3 10.1 1.0 N C:CYS415 4.3 11.6 1.0 CG C:PRO386 4.4 4.0 1.0 SG C:CYS409 4.4 8.3 1.0 CZ C:PHE429 4.6 3.3 1.0 CB C:PRO386 4.6 0.0 1.0 CA C:CYS415 4.6 3.7 1.0 SG C:CYS380 4.7 26.6 1.0 SG C:CYS412 4.7 13.6 1.0 CB C:CYS380 5.0 1.5 1.0

Iron binding site 10 out of 18 in the Cryo-Em Structure of the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced


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 the Nadh:Ferredoxin Oxidoreductase Rnf From Azotobacter Vinelandii, Dithionite Reduced within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:21.5 occ:1.00 FE4 C:SF4502 0.0 21.5 1.0 SG C:CYS380 2.3 26.6 1.0 S3 C:SF4502 2.3 15.7 1.0 S2 C:SF4502 2.3 37.7 1.0 S1 C:SF4502 2.3 15.1 1.0 FE3 C:SF4502 2.7 19.2 1.0 FE2 C:SF4502 2.7 8.6 1.0 FE1 C:SF4502 2.7 30.9 1.0 CB C:CYS380 3.3 1.5 1.0 S4 C:SF4502 3.9 17.9 1.0 CA C:CYS380 3.9 0.0 1.0 CD C:PRO381 4.0 14.3 1.0 CD1 C:LEU384 4.1 0.6 1.0 SG C:CYS415 4.4 27.2 1.0 N C:PRO381 4.4 4.7 1.0 C C:CYS380 4.5 8.1 1.0 SG C:CYS412 4.6 13.6 1.0 CG C:MET382 4.7 2.3 1.0 CG C:LEU384 4.7 4.7 1.0 CG C:PRO386 4.8 4.0 1.0 N C:MET382 4.8 3.0 1.0 CB C:LEU384 4.8 5.1 1.0 SG C:CYS409 5.0 8.3 1.0

L.Zhang, O.Einsle. Architecture of the RNF1 Complex That Drives Biological Nitrogen Fixation. Nat.Chem.Biol. 2024.
ISSN: ESSN 1552-4469
PubMed: 38890433
DOI: 10.1038/S41589-024-01641-1