Iron in PDB 10zk: Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)

All present enzymatic activity of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry):
1.18.6.1;

The structure of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Molybdenum	(Mo)	2 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40;

Binding sites:

The binding sites of Iron atom in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) (pdb code 10zk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 40 binding sites of Iron where determined in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry), PDB code: 10zk:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:38.6 occ:1.00 FE1 A:ICS502 0.0 38.6 1.0 S2A A:ICS502 2.3 34.4 1.0 SG A:CYS291 2.3 25.2 1.0 S4A A:ICS502 2.3 29.8 1.0 S1A A:ICS502 2.3 27.8 1.0 FE4 A:ICS502 2.7 37.2 1.0 FE3 A:ICS502 2.7 36.4 1.0 FE2 A:ICS502 2.7 32.9 1.0 CB A:CYS291 3.3 21.8 1.0 CX A:ICS502 3.4 32.6 1.0 OG A:SER294 3.7 21.8 1.0 CB A:LEU374 4.2 28.3 1.0 CB A:SER294 4.3 22.1 1.0 CA A:CYS291 4.6 22.3 1.0 CE2 A:TYR245 4.6 22.8 1.0 N A:SER294 4.6 24.7 1.0 CB A:ARG293 4.7 28.4 1.0 CD2 A:LEU374 4.8 26.0 1.0 S2B A:ICS502 4.8 25.1 1.0 S3A A:ICS502 4.8 23.2 1.0 S5A A:ICS502 4.8 28.5 1.0 FE6 A:ICS502 5.0 28.9 1.0 FE7 A:ICS502 5.0 31.5 1.0

Iron binding site 2 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:32.9 occ:1.00 FE2 A:ICS502 0.0 32.9 1.0 CX A:ICS502 2.0 32.6 1.0 S2B A:ICS502 2.2 25.1 1.0 S2A A:ICS502 2.2 34.4 1.0 S1A A:ICS502 2.3 27.8 1.0 FE6 A:ICS502 2.6 28.9 1.0 FE4 A:ICS502 2.7 37.2 1.0 FE1 A:ICS502 2.7 38.6 1.0 FE3 A:ICS502 2.7 36.4 1.0 FE5 A:ICS502 3.7 37.9 1.0 FE7 A:ICS502 3.7 31.5 1.0 S4A A:ICS502 3.9 29.8 1.0 CE1 A:HIS211 4.0 20.0 1.0 CZ A:PHE397 4.1 24.1 1.0 NE2 A:HIS211 4.2 20.0 1.0 S3B A:ICS502 4.2 33.2 1.0 S1B A:ICS502 4.2 28.8 1.0 CG1 A:VAL86 4.5 19.2 1.0 S3A A:ICS502 4.5 23.2 1.0 S5A A:ICS502 4.5 28.5 1.0 CE1 A:PHE397 4.6 22.7 1.0 SG A:CYS291 4.7 25.2 1.0 CG2 A:VAL86 4.9 20.7 1.0 OG A:SER294 4.9 21.8 1.0 CB A:SER294 4.9 22.1 1.0

Iron binding site 3 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:36.4 occ:1.00 FE3 A:ICS502 0.0 36.4 1.0 CX A:ICS502 2.0 32.6 1.0 S5A A:ICS502 2.2 28.5 1.0 S4A A:ICS502 2.2 29.8 1.0 S2A A:ICS502 2.3 34.4 1.0 FE7 A:ICS502 2.6 31.5 1.0 FE4 A:ICS502 2.6 37.2 1.0 FE1 A:ICS502 2.7 38.6 1.0 FE2 A:ICS502 2.7 32.9 1.0 FE6 A:ICS502 3.7 28.9 1.0 FE5 A:ICS502 3.7 37.9 1.0 S1A A:ICS502 3.9 27.8 1.0 NH2 A:ARG112 4.2 23.7 1.0 S3B A:ICS502 4.2 33.2 1.0 S4B A:ICS502 4.2 36.4 1.0 CD2 A:TYR245 4.3 23.7 1.0 CE2 A:TYR245 4.5 22.8 1.0 S2B A:ICS502 4.5 25.1 1.0 S3A A:ICS502 4.5 23.2 1.0 SG A:CYS291 4.7 25.2 1.0 NE A:ARG375 5.0 30.1 1.0 NH2 A:ARG375 5.0 28.0 1.0

Iron binding site 4 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:37.2 occ:1.00 FE4 A:ICS502 0.0 37.2 1.0 CX A:ICS502 2.0 32.6 1.0 S3A A:ICS502 2.2 23.2 1.0 S4A A:ICS502 2.3 29.8 1.0 S1A A:ICS502 2.3 27.8 1.0 FE5 A:ICS502 2.6 37.9 1.0 FE3 A:ICS502 2.6 36.4 1.0 FE2 A:ICS502 2.7 32.9 1.0 FE1 A:ICS502 2.7 38.6 1.0 FE7 A:ICS502 3.7 31.5 1.0 FE6 A:ICS502 3.7 28.9 1.0 S2A A:ICS502 3.8 34.4 1.0 N A:LEU374 3.8 29.0 1.0 CB A:LEU374 3.9 28.3 1.0 N A:GLY373 4.1 23.6 1.0 S4B A:ICS502 4.3 36.4 1.0 S1B A:ICS502 4.3 28.8 1.0 CA A:LEU374 4.5 27.6 1.0 S5A A:ICS502 4.5 28.5 1.0 S2B A:ICS502 4.5 25.1 1.0 C A:GLY373 4.5 29.3 1.0 SG A:CYS291 4.6 25.2 1.0 CA A:GLY373 4.7 24.1 1.0 N A:ARG375 4.7 28.4 1.0 CG A:ARG375 4.8 31.4 1.0 NE A:ARG375 5.0 30.1 1.0

Iron binding site 5 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:37.9 occ:1.00 FE5 A:ICS502 0.0 37.9 1.0 CX A:ICS502 2.0 32.6 1.0 S4B A:ICS502 2.2 36.4 1.0 S3A A:ICS502 2.3 23.2 1.0 S1B A:ICS502 2.3 28.8 1.0 FE4 A:ICS502 2.6 37.2 1.0 FE7 A:ICS502 2.6 31.5 1.0 FE6 A:ICS502 2.6 28.9 1.0 MO1 A:ICS502 2.7 51.0 1.0 FE2 A:ICS502 3.7 32.9 1.0 FE3 A:ICS502 3.7 36.4 1.0 S3B A:ICS502 3.9 33.2 1.0 CG1 A:VAL371 4.0 29.1 1.0 N A:GLY372 4.1 25.5 1.0 ND1 A:HIS458 4.2 26.4 1.0 S1A A:ICS502 4.3 27.8 1.0 CA A:GLY372 4.3 24.2 1.0 S4A A:ICS502 4.3 29.8 1.0 S2B A:ICS502 4.5 25.1 1.0 S5A A:ICS502 4.5 28.5 1.0 CE1 A:HIS458 4.5 28.2 1.0 N A:GLY373 4.5 23.6 1.0 CD A:ARG375 4.6 31.5 1.0 NE A:ARG375 4.7 30.1 1.0 CG A:ARG375 5.0 31.4 1.0 C A:GLY372 5.0 25.1 1.0

Iron binding site 6 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:28.9 occ:1.00 FE6 A:ICS502 0.0 28.9 1.0 CX A:ICS502 2.0 32.6 1.0 S2B A:ICS502 2.2 25.1 1.0 S3B A:ICS502 2.2 33.2 1.0 S1B A:ICS502 2.2 28.8 1.0 FE2 A:ICS502 2.6 32.9 1.0 FE7 A:ICS502 2.6 31.5 1.0 FE5 A:ICS502 2.6 37.9 1.0 MO1 A:ICS502 2.7 51.0 1.0 O7 A:HCA501 3.6 26.7 1.0 FE3 A:ICS502 3.7 36.4 1.0 FE4 A:ICS502 3.7 37.2 1.0 S4B A:ICS502 3.8 36.4 1.0 OE1 A:GLN207 4.2 29.0 1.0 S2A A:ICS502 4.2 34.4 1.0 CZ A:PHE397 4.3 24.1 1.0 S1A A:ICS502 4.3 27.8 1.0 S5A A:ICS502 4.5 28.5 1.0 CG2 A:VAL86 4.5 20.7 1.0 S3A A:ICS502 4.5 23.2 1.0 CE2 A:PHE397 4.8 25.1 1.0 O1 A:HCA501 5.0 26.7 1.0 FE1 A:ICS502 5.0 38.6 1.0 C3 A:HCA501 5.0 30.0 1.0

Iron binding site 7 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:31.5 occ:1.00 FE7 A:ICS502 0.0 31.5 1.0 CX A:ICS502 2.0 32.6 1.0 S5A A:ICS502 2.2 28.5 1.0 S4B A:ICS502 2.2 36.4 1.0 S3B A:ICS502 2.2 33.2 1.0 FE3 A:ICS502 2.6 36.4 1.0 FE6 A:ICS502 2.6 28.9 1.0 FE5 A:ICS502 2.6 37.9 1.0 MO1 A:ICS502 2.7 51.0 1.0 FE2 A:ICS502 3.7 32.9 1.0 FE4 A:ICS502 3.7 37.2 1.0 S1B A:ICS502 3.8 28.8 1.0 NH2 A:ARG112 4.3 23.7 1.0 S2A A:ICS502 4.3 34.4 1.0 S4A A:ICS502 4.3 29.8 1.0 NE A:ARG112 4.3 22.4 1.0 S2B A:ICS502 4.4 25.1 1.0 CZ A:ARG375 4.4 28.8 1.0 NH2 A:ARG375 4.5 28.0 1.0 S3A A:ICS502 4.5 23.2 1.0 O6 A:HCA501 4.7 32.7 1.0 NE A:ARG375 4.7 30.1 1.0 NH1 A:ARG375 4.7 28.5 1.0 O7 A:HCA501 4.7 26.7 1.0 CZ A:ARG112 4.8 21.7 1.0 FE1 A:ICS502 5.0 38.6 1.0 O A:HIS458 5.0 28.5 1.0

Iron binding site 8 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:58.9 occ:1.00 FE1 B:CLF601 0.0 58.9 1.0 SG A:CYS170 1.9 21.8 1.0 S3A B:CLF601 2.3 39.5 1.0 S2A B:CLF601 2.3 46.8 1.0 S1 B:CLF601 2.4 52.4 1.0 FE2 B:CLF601 2.5 75.1 1.0 FE4 B:CLF601 2.6 53.5 1.0 FE3 B:CLF601 2.8 58.8 1.0 CB A:CYS170 3.3 19.7 1.0 CA A:GLY201 3.7 19.8 1.0 S4A B:CLF601 3.8 55.3 1.0 N A:CYS170 3.9 22.0 1.0 SG B:CYS94 4.0 25.4 1.0 N A:GLY201 4.0 18.5 1.0 CA A:CYS170 4.1 19.7 1.0 FE8 B:CLF601 4.4 53.6 1.0 SG A:CYS104 4.4 23.1 1.0 OG B:SER91 4.6 28.5 1.0 CB B:SER91 4.6 25.2 1.0 FE5 B:CLF601 4.6 66.3 1.0 C A:GLY201 4.7 18.6 1.0 SG B:CYS152 4.8 26.7 1.0 FE6 B:CLF601 4.9 71.6 1.0 C A:GLU169 4.9 21.1 1.0 N A:PHE202 5.0 16.2 1.0

Iron binding site 9 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:75.1 occ:1.00 FE2 B:CLF601 0.0 75.1 1.0 SG B:CYS94 2.1 25.4 1.0 S4A B:CLF601 2.3 55.3 1.0 S2A B:CLF601 2.3 46.8 1.0 S1 B:CLF601 2.5 52.4 1.0 FE1 B:CLF601 2.5 58.9 1.0 FE4 B:CLF601 2.6 53.5 1.0 FE3 B:CLF601 2.7 58.8 1.0 FE8 B:CLF601 2.9 53.6 1.0 N B:CYS94 3.3 19.9 1.0 CB B:CYS94 3.4 19.4 1.0 CA B:CYS94 3.5 17.5 1.0 S3A B:CLF601 3.8 39.5 1.0 FE5 B:CLF601 3.9 66.3 1.0 S4B B:CLF601 3.9 41.9 1.0 C B:GLY93 4.1 18.4 1.0 SG A:CYS170 4.2 21.8 1.0 SG A:CYS104 4.4 23.1 1.0 CB B:SER91 4.5 25.2 1.0 FE6 B:CLF601 4.5 71.6 1.0 CA B:GLY93 4.7 14.7 1.0 O B:GLY93 4.7 20.3 1.0 SG A:CYS78 4.8 21.0 1.0

Iron binding site 10 out of 40 in the Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryoem Structure of Gluconacetobacter Diazotrophicus Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:58.8 occ:1.00 FE3 B:CLF601 0.0 58.8 1.0 S4A B:CLF601 2.2 55.3 1.0 S2A B:CLF601 2.3 46.8 1.0 S3A B:CLF601 2.3 39.5 1.0 SG A:CYS78 2.3 21.0 1.0 FE4 B:CLF601 2.7 53.5 1.0 FE2 B:CLF601 2.7 75.1 1.0 FE1 B:CLF601 2.8 58.9 1.0 CB A:CYS78 3.0 21.9 1.0 CA A:GLY201 3.9 19.8 1.0 CB A:TYR80 3.9 19.1 1.0 S1 B:CLF601 4.2 52.4 1.0 CD2 A:TYR80 4.4 19.0 1.0 SG A:CYS170 4.5 21.8 1.0 CA B:GLY93 4.5 14.7 1.0 CA A:CYS78 4.5 19.5 1.0 CG A:TYR80 4.5 19.9 1.0 C B:GLY93 4.6 18.4 1.0 SG A:CYS104 4.6 23.1 1.0 N B:CYS94 4.6 19.9 1.0 N A:GLY201 4.6 18.5 1.0 SG B:CYS94 4.7 25.4 1.0 N A:TYR80 4.8 18.8 1.0 CE2 B:TYR97 4.9 12.9 1.0 CA A:TYR80 4.9 18.4 1.0 C A:GLY201 5.0 18.6 1.0

Y.Li, S.M.Narehood, B.D.Cook, K.L.Mcguire, M.A.Herzik Jr., F.A.Tezcan. Structural and Functional Characterization of Heterologous Nitrogenase Complexes. Biochemistry 2026.
ISSN: ISSN 0006-2960
PubMed: 42390130
DOI: 10.1021/ACS.BIOCHEM.6C00360