Iron in PDB 4xpi: Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer

All present enzymatic activity of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer:
1.18.6.1;

The structure of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer, PDB code: 4xpi was solved by K.Danyal, A.J.Rasmusen, S.M.Keable, S.Shaw, O.Zadvornyy, S.Duval, D.R.Dean, S.Raugei, J.W.Peters, L.C.Seefeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.804, 130.830, 108.110, 90.00, 111.14, 90.00
R / Rfree (%)	21.3 / 26.4

The structure of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Calcium	(Ca)	2 atoms

Pages:

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

Binding sites:

The binding sites of Iron atom in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer (pdb code 4xpi). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer, PDB code: 4xpi:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:29.4 occ:1.00 FE1 A:ICS502 0.0 29.4 1.0 S4A A:ICS502 2.1 34.8 1.0 S2A A:ICS502 2.1 37.3 1.0 SG A:CYS275 2.2 35.5 1.0 S1A A:ICS502 2.2 33.2 1.0 FE3 A:ICS502 2.8 32.2 1.0 FE4 A:ICS502 2.9 30.2 1.0 FE2 A:ICS502 2.9 33.4 1.0 CB A:CYS275 3.0 39.7 1.0 CX A:ICS502 3.5 25.9 1.0 OG A:SER278 3.9 32.6 1.0 CA A:CYS275 4.3 36.4 1.0 CB A:LEU358 4.3 29.5 1.0 CE2 A:TYR229 4.3 30.5 1.0 CB A:SER278 4.3 33.8 1.0 CD2 A:LEU358 4.6 31.5 1.0 CD2 A:TYR229 4.8 27.1 1.0 N A:SER278 4.9 34.1 1.0 S5A A:ICS502 4.9 30.0 1.0 C A:CYS275 4.9 34.5 1.0

Iron binding site 2 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:33.4 occ:1.00 FE2 A:ICS502 0.0 33.4 1.0 CX A:ICS502 1.8 25.9 1.0 S1A A:ICS502 2.1 33.2 1.0 S2A A:ICS502 2.1 37.3 1.0 S2B A:ICS502 2.3 34.0 1.0 FE6 A:ICS502 2.4 30.6 1.0 FE4 A:ICS502 2.6 30.2 1.0 FE3 A:ICS502 2.7 32.2 1.0 FE1 A:ICS502 2.9 29.4 1.0 FE5 A:ICS502 3.5 32.0 1.0 S4A A:ICS502 3.5 34.8 1.0 FE7 A:ICS502 3.6 29.8 1.0 CZ A:PHE381 3.9 31.7 1.0 S1B A:ICS502 3.9 35.3 1.0 S3B A:ICS502 4.1 31.7 1.0 NE2 A:HIS195 4.3 41.5 1.0 S3A A:ICS502 4.4 35.6 1.0 CE1 A:HIS195 4.4 45.7 1.0 S5A A:ICS502 4.5 30.0 1.0 CG1 A:VAL70 4.5 27.2 1.0 CE1 A:PHE381 4.6 32.4 1.0 SG A:CYS275 4.7 35.5 1.0 CE2 A:PHE381 4.8 34.4 1.0 S4B A:ICS502 4.9 36.0 1.0 N A:GLY357 5.0 28.7 1.0 MO1 A:ICS502 5.0 29.0 1.0

Iron binding site 3 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:32.2 occ:1.00 FE3 A:ICS502 0.0 32.2 1.0 CX A:ICS502 1.9 25.9 1.0 S4A A:ICS502 2.1 34.8 1.0 S2A A:ICS502 2.1 37.3 1.0 S5A A:ICS502 2.2 30.0 1.0 FE7 A:ICS502 2.5 29.8 1.0 FE4 A:ICS502 2.7 30.2 1.0 FE2 A:ICS502 2.7 33.4 1.0 FE1 A:ICS502 2.8 29.4 1.0 FE5 A:ICS502 3.6 32.0 1.0 S1A A:ICS502 3.6 33.2 1.0 FE6 A:ICS502 3.6 30.6 1.0 CD2 A:TYR229 4.0 27.1 1.0 NH2 A:ARG96 4.0 39.0 1.0 S4B A:ICS502 4.1 36.0 1.0 O A:HOH786 4.1 28.9 1.0 S3B A:ICS502 4.1 31.7 1.0 CE2 A:TYR229 4.3 30.5 1.0 S3A A:ICS502 4.6 35.6 1.0 S2B A:ICS502 4.6 34.0 1.0 SG A:CYS275 4.9 35.5 1.0

Iron binding site 4 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:30.2 occ:1.00 FE4 A:ICS502 0.0 30.2 1.0 CX A:ICS502 2.0 25.9 1.0 S1A A:ICS502 2.1 33.2 1.0 S4A A:ICS502 2.1 34.8 1.0 S3A A:ICS502 2.2 35.6 1.0 FE5 A:ICS502 2.5 32.0 1.0 FE2 A:ICS502 2.6 33.4 1.0 FE3 A:ICS502 2.7 32.2 1.0 FE1 A:ICS502 2.9 29.4 1.0 S2A A:ICS502 3.5 37.3 1.0 FE6 A:ICS502 3.6 30.6 1.0 FE7 A:ICS502 3.7 29.8 1.0 N A:GLY357 4.0 28.7 1.0 S1B A:ICS502 4.1 35.3 1.0 N A:LEU358 4.1 32.0 1.0 S4B A:ICS502 4.1 36.0 1.0 CB A:LEU358 4.1 29.5 1.0 S2B A:ICS502 4.5 34.0 1.0 S5A A:ICS502 4.6 30.0 1.0 CA A:GLY357 4.6 32.2 1.0 C A:GLY357 4.6 32.7 1.0 CA A:LEU358 4.7 31.3 1.0 N A:ARG359 4.7 30.2 1.0 SG A:CYS275 4.8 35.5 1.0 CG A:ARG359 4.8 31.6 1.0 C A:GLY356 4.9 25.7 1.0 CZ A:PHE381 4.9 31.7 1.0 CA A:GLY356 5.0 25.6 1.0 CD A:ARG359 5.0 32.0 1.0

Iron binding site 5 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:32.0 occ:1.00 FE5 A:ICS502 0.0 32.0 1.0 CX A:ICS502 2.0 25.9 1.0 S4B A:ICS502 2.1 36.0 1.0 S1B A:ICS502 2.1 35.3 1.0 S3A A:ICS502 2.2 35.6 1.0 FE4 A:ICS502 2.5 30.2 1.0 FE6 A:ICS502 2.6 30.6 1.0 FE7 A:ICS502 2.6 29.8 1.0 MO1 A:ICS502 2.8 29.0 1.0 FE2 A:ICS502 3.5 33.4 1.0 FE3 A:ICS502 3.6 32.2 1.0 S3B A:ICS502 3.6 31.7 1.0 ND1 A:HIS442 3.8 26.4 1.0 S4A A:ICS502 4.1 34.8 1.0 S1A A:ICS502 4.1 33.2 1.0 N A:GLY356 4.3 24.9 1.0 CA A:GLY356 4.3 25.6 1.0 CE1 A:HIS442 4.3 28.5 1.0 CG2 A:ILE355 4.3 27.6 1.0 S2B A:ICS502 4.5 34.0 1.0 S5A A:ICS502 4.5 30.0 1.0 N A:GLY357 4.7 28.7 1.0 O7 A:HCA501 4.7 29.6 1.0 CG A:HIS442 4.7 30.2 1.0 CD A:ARG359 4.7 32.0 1.0 O6 A:HCA501 4.8 27.9 1.0 S2A A:ICS502 4.9 37.3 1.0

Iron binding site 6 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:30.6 occ:1.00 FE6 A:ICS502 0.0 30.6 1.0 CX A:ICS502 2.0 25.9 1.0 S3B A:ICS502 2.1 31.7 1.0 S1B A:ICS502 2.1 35.3 1.0 S2B A:ICS502 2.2 34.0 1.0 FE2 A:ICS502 2.4 33.4 1.0 FE7 A:ICS502 2.6 29.8 1.0 FE5 A:ICS502 2.6 32.0 1.0 MO1 A:ICS502 2.7 29.0 1.0 S4B A:ICS502 3.5 36.0 1.0 FE4 A:ICS502 3.6 30.2 1.0 FE3 A:ICS502 3.6 32.2 1.0 O7 A:HCA501 3.8 29.6 1.0 S2A A:ICS502 4.0 37.3 1.0 S1A A:ICS502 4.2 33.2 1.0 CZ A:PHE381 4.3 31.7 1.0 O2 A:HCA501 4.3 32.2 1.0 S5A A:ICS502 4.4 30.0 1.0 S3A A:ICS502 4.5 35.6 1.0 O6 A:HCA501 4.5 27.9 1.0 CE2 A:PHE381 4.5 34.4 1.0 CG2 A:VAL70 4.6 25.8 1.0 ND1 A:HIS442 4.7 26.4 1.0 C3 A:HCA501 4.9 36.8 1.0 S4A A:ICS502 5.0 34.8 1.0

Iron binding site 7 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:29.8 occ:1.00 FE7 A:ICS502 0.0 29.8 1.0 CX A:ICS502 2.0 25.9 1.0 S3B A:ICS502 2.1 31.7 1.0 S4B A:ICS502 2.1 36.0 1.0 S5A A:ICS502 2.2 30.0 1.0 FE3 A:ICS502 2.5 32.2 1.0 FE6 A:ICS502 2.6 30.6 1.0 FE5 A:ICS502 2.6 32.0 1.0 MO1 A:ICS502 2.8 29.0 1.0 S1B A:ICS502 3.6 35.3 1.0 FE2 A:ICS502 3.6 33.4 1.0 O A:HOH745 3.7 34.1 1.0 FE4 A:ICS502 3.7 30.2 1.0 O6 A:HCA501 3.8 27.9 1.0 S2A A:ICS502 4.0 37.3 1.0 NH2 A:ARG96 4.1 39.0 1.0 S4A A:ICS502 4.1 34.8 1.0 NE A:ARG96 4.2 31.8 1.0 S2B A:ICS502 4.5 34.0 1.0 S3A A:ICS502 4.6 35.6 1.0 O7 A:HCA501 4.6 29.6 1.0 CZ A:ARG96 4.6 33.8 1.0 C7 A:HCA501 4.8 30.3 1.0 ND1 A:HIS442 4.8 26.4 1.0 CZ A:ARG359 4.8 30.9 1.0 NH1 A:ARG359 4.8 29.9 1.0 NH2 A:ARG359 5.0 34.5 1.0

Iron binding site 8 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe504 b:30.2 occ:0.88 FE1 A:1CL504 0.0 30.2 0.9 S2A A:1CL504 2.1 35.6 0.9 S3A A:1CL504 2.1 35.4 0.9 S1 A:1CL504 2.1 35.0 0.9 SG A:CYS154 2.3 33.2 1.0 FE2 A:1CL504 2.7 27.7 0.9 FE4 A:1CL504 2.9 30.3 0.9 FE3 A:1CL504 3.0 27.6 0.9 CB A:CYS154 3.3 35.1 1.0 S4A A:1CL504 3.5 37.8 0.9 N A:CYS154 3.9 37.5 1.0 CA A:GLY185 3.9 35.7 1.0 O B:HOH746 4.0 34.5 1.0 OG B:SER92 4.1 39.4 0.4 N A:GLY185 4.1 36.7 1.0 CA A:CYS154 4.1 37.2 1.0 FE8 A:1CL504 4.2 27.2 0.9 CB B:SER92 4.2 38.1 1.0 SG B:CYS95 4.3 28.6 1.0 C A:GLY185 4.7 36.3 1.0 SG A:CYS88 4.8 32.9 1.0

Iron binding site 9 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe504 b:27.7 occ:0.88 FE2 A:1CL504 0.0 27.7 0.9 S2A A:1CL504 2.1 35.6 0.9 S4A A:1CL504 2.1 37.8 0.9 S1 A:1CL504 2.2 35.0 0.9 SG B:CYS95 2.3 28.6 1.0 FE8 A:1CL504 2.7 27.2 0.9 FE1 A:1CL504 2.7 30.2 0.9 FE4 A:1CL504 2.9 30.3 0.9 N B:CYS95 3.0 32.6 1.0 FE3 A:1CL504 3.1 27.6 0.9 CA B:CYS95 3.3 32.2 1.0 CB B:CYS95 3.4 30.1 1.0 S3A A:1CL504 3.6 35.4 0.9 C B:GLY94 3.7 32.2 1.0 S4B A:1CL504 3.8 33.3 0.9 CA B:GLY94 4.3 31.4 1.0 CB B:SER92 4.3 38.1 1.0 O B:GLY94 4.4 29.4 1.0 N B:GLY94 4.6 35.7 1.0 O B:HOH746 4.7 34.5 1.0 S3B A:1CL504 4.7 41.3 0.9 SG A:CYS88 4.8 32.9 1.0 SG A:CYS154 4.8 33.2 1.0 O B:SER92 4.8 42.4 1.0 C B:CYS95 4.8 31.4 1.0 FE5 A:1CL504 4.9 28.6 0.9 SG A:CYS62 4.9 35.4 1.0

Iron binding site 10 out of 30 in the Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Fe Protein Independent Substrate Reduction By Nitrogenase Variants Altered in Intramolecular Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe504 b:27.6 occ:0.88 FE3 A:1CL504 0.0 27.6 0.9 S4A A:1CL504 2.1 37.8 0.9 S3A A:1CL504 2.1 35.4 0.9 S2A A:1CL504 2.1 35.6 0.9 SG A:CYS62 2.1 35.4 1.0 FE4 A:1CL504 3.0 30.3 0.9 FE1 A:1CL504 3.0 30.2 0.9 FE2 A:1CL504 3.1 27.7 0.9 CB A:CYS62 3.1 31.2 1.0 CA A:GLY185 3.9 35.7 1.0 CB A:TYR64 3.9 32.1 1.0 S1 A:1CL504 4.0 35.0 0.9 CA B:GLY94 4.2 31.4 1.0 C B:GLY94 4.4 32.2 1.0 O B:HOH910 4.5 40.3 1.0 CA A:CYS62 4.5 31.7 1.0 N A:GLY185 4.6 36.7 1.0 CG A:TYR64 4.6 34.4 1.0 CD2 A:TYR64 4.6 36.1 1.0 N B:CYS95 4.6 32.6 1.0 N A:TYR64 4.7 31.6 1.0 O A:HOH738 4.9 40.1 1.0 N B:GLY94 4.9 35.7 1.0 CA A:TYR64 4.9 31.5 1.0 O B:GLY94 4.9 29.4 1.0 SG A:CYS154 5.0 33.2 1.0 C A:CYS62 5.0 30.4 1.0

K.Danyal, A.J.Rasmussen, S.M.Keable, B.S.Inglet, S.Shaw, O.A.Zadvornyy, S.Duval, D.R.Dean, S.Raugei, J.W.Peters, L.C.Seefeldt. Fe Protein-Independent Substrate Reduction By Nitrogenase Mofe Protein Variants. Biochemistry V. 54 2456 2015.
ISSN: ISSN 0006-2960
PubMed: 25831270
DOI: 10.1021/ACS.BIOCHEM.5B00140