Iron in PDB 1m34: Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate

All present enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate:
1.18.6.1;

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1m34 was solved by B.Schmid, O.Einsle, H.-J.Chiu, A.Willing, M.Yoshida, J.B.Howard, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	326.100, 75.800, 312.200, 90.00, 102.60, 90.00
R / Rfree (%)	20 / 23.6

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate also contains other interesting chemical elements:

Fluorine	(F)	32 atoms
Molybdenum	(Mo)	4 atoms
Magnesium	(Mg)	8 atoms
Aluminium	(Al)	8 atoms
Calcium	(Ca)	4 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 50; Page 6, Binding sites: 51 - 60; Page 7, Binding sites: 61 - 70; Page 8, Binding sites: 71 - 76;

Binding sites:

The binding sites of Iron atom in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate (pdb code 1m34). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 76 binding sites of Iron where determined in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1m34:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:21.9 occ:1.00 FE1 A:CFM2096 0.0 21.9 1.0 S4A A:CFM2096 2.3 22.6 1.0 SG A:CYS275 2.3 19.7 1.0 S1A A:CFM2096 2.3 20.9 1.0 S2A A:CFM2096 2.3 18.7 1.0 FE4 A:CFM2096 2.7 24.3 1.0 FE2 A:CFM2096 2.7 21.5 1.0 FE3 A:CFM2096 2.8 22.7 1.0 CB A:CYS275 3.3 25.7 1.0 CB A:LEU358 4.1 25.8 1.0 OG A:SER278 4.4 21.8 1.0 CB A:SER278 4.5 22.0 1.0 CE2 A:TYR229 4.5 22.8 1.0 CA A:CYS275 4.5 26.7 1.0 CD2 A:LEU358 4.8 28.4 1.0 S2B A:CFM2096 4.9 20.1 1.0 S5 A:CFM2096 4.9 18.8 1.0 FE7 A:CFM2096 4.9 20.4 1.0 N A:SER278 4.9 25.3 1.0 S3A A:CFM2096 4.9 23.8 1.0 CD2 A:TYR229 4.9 25.6 1.0 N A:LEU358 4.9 23.4 1.0 O A:HOH2221 5.0 47.0 1.0 FE5 A:CFM2096 5.0 25.5 1.0 FE6 A:CFM2096 5.0 21.1 1.0

Iron binding site 2 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:21.5 occ:1.00 FE2 A:CFM2096 0.0 21.5 1.0 S2B A:CFM2096 2.3 20.1 1.0 S1A A:CFM2096 2.3 20.9 1.0 S2A A:CFM2096 2.3 18.7 1.0 FE6 A:CFM2096 2.5 21.1 1.0 FE3 A:CFM2096 2.6 22.7 1.0 FE1 A:CFM2096 2.7 21.9 1.0 FE4 A:CFM2096 2.7 24.3 1.0 FE7 A:CFM2096 3.6 20.4 1.0 FE5 A:CFM2096 3.6 25.5 1.0 S4A A:CFM2096 3.8 22.6 1.0 S3B A:CFM2096 4.1 23.4 1.0 CZ A:PHE381 4.2 19.0 1.0 NE2 A:HIS195 4.2 27.5 1.0 S1B A:CFM2096 4.3 24.5 1.0 CE1 A:HIS195 4.3 25.3 1.0 CE1 A:PHE381 4.6 22.1 1.0 S5 A:CFM2096 4.6 18.8 1.0 S3A A:CFM2096 4.6 23.8 1.0 SG A:CYS275 4.7 19.7 1.0 CG2 A:VAL70 4.9 27.0 1.0 CB A:VAL70 5.0 28.7 1.0 CG1 A:VAL70 5.0 24.6 1.0

Iron binding site 3 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:22.7 occ:1.00 FE3 A:CFM2096 0.0 22.7 1.0 S5 A:CFM2096 2.2 18.8 1.0 S2A A:CFM2096 2.3 18.7 1.0 S4A A:CFM2096 2.3 22.6 1.0 FE7 A:CFM2096 2.3 20.4 1.0 FE2 A:CFM2096 2.6 21.5 1.0 FE4 A:CFM2096 2.7 24.3 1.0 FE1 A:CFM2096 2.8 21.9 1.0 FE6 A:CFM2096 3.5 21.1 1.0 FE5 A:CFM2096 3.6 25.5 1.0 S1A A:CFM2096 3.9 20.9 1.0 S3B A:CFM2096 4.0 23.4 1.0 NH2 A:ARG96 4.1 29.0 1.0 O A:HOH2099 4.1 17.7 1.0 CD2 A:TYR229 4.1 25.6 1.0 S4B A:CFM2096 4.2 25.4 1.0 S2B A:CFM2096 4.5 20.1 1.0 CE2 A:TYR229 4.5 22.8 1.0 S3A A:CFM2096 4.5 23.8 1.0 SG A:CYS275 4.9 19.7 1.0 MO1 A:CFM2096 5.0 26.6 1.0

Iron binding site 4 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:24.3 occ:1.00 FE4 A:CFM2096 0.0 24.3 1.0 S4A A:CFM2096 2.3 22.6 1.0 S1A A:CFM2096 2.3 20.9 1.0 S3A A:CFM2096 2.3 23.8 1.0 FE5 A:CFM2096 2.6 25.5 1.0 FE1 A:CFM2096 2.7 21.9 1.0 FE3 A:CFM2096 2.7 22.7 1.0 FE2 A:CFM2096 2.7 21.5 1.0 FE7 A:CFM2096 3.7 20.4 1.0 FE6 A:CFM2096 3.7 21.1 1.0 S2A A:CFM2096 3.9 18.7 1.0 N A:LEU358 3.9 23.4 1.0 CB A:LEU358 4.0 25.8 1.0 N A:GLY357 4.0 24.2 1.0 S4B A:CFM2096 4.3 25.4 1.0 S1B A:CFM2096 4.4 24.5 1.0 CA A:LEU358 4.5 25.0 1.0 S2B A:CFM2096 4.6 20.1 1.0 C A:GLY357 4.6 24.8 1.0 S5 A:CFM2096 4.6 18.8 1.0 N A:ARG359 4.6 26.3 1.0 SG A:CYS275 4.7 19.7 1.0 CA A:GLY357 4.7 24.0 1.0 CG A:ARG359 4.8 28.0 1.0 CA A:GLY356 4.9 22.6 1.0 C A:GLY356 5.0 24.2 1.0

Iron binding site 5 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:25.5 occ:1.00 FE5 A:CFM2096 0.0 25.5 1.0 S3A A:CFM2096 2.3 23.8 1.0 S4B A:CFM2096 2.3 25.4 1.0 S1B A:CFM2096 2.3 24.5 1.0 FE6 A:CFM2096 2.5 21.1 1.0 FE4 A:CFM2096 2.6 24.3 1.0 FE7 A:CFM2096 2.7 20.4 1.0 MO1 A:CFM2096 2.9 26.6 1.0 FE3 A:CFM2096 3.6 22.7 1.0 FE2 A:CFM2096 3.6 21.5 1.0 S3B A:CFM2096 3.8 23.4 1.0 ND1 A:HIS442 4.0 25.3 1.0 N A:GLY356 4.1 23.6 1.0 CA A:GLY356 4.1 22.6 1.0 S1A A:CFM2096 4.2 20.9 1.0 CG2 A:ILE355 4.3 21.6 1.0 S4A A:CFM2096 4.3 22.6 1.0 S2B A:CFM2096 4.4 20.1 1.0 S5 A:CFM2096 4.6 18.8 1.0 CE1 A:HIS442 4.6 26.9 1.0 N A:GLY357 4.7 24.2 1.0 CD A:ARG359 4.9 26.8 1.0 FE1 A:CFM2096 5.0 21.9 1.0 CZ A:PHE381 5.0 19.0 1.0

Iron binding site 6 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:21.1 occ:1.00 FE6 A:CFM2096 0.0 21.1 1.0 S3B A:CFM2096 2.2 23.4 1.0 S2B A:CFM2096 2.3 20.1 1.0 S1B A:CFM2096 2.3 24.5 1.0 FE2 A:CFM2096 2.5 21.5 1.0 FE5 A:CFM2096 2.5 25.5 1.0 FE7 A:CFM2096 2.6 20.4 1.0 MO1 A:CFM2096 2.7 26.6 1.0 FE3 A:CFM2096 3.5 22.7 1.0 FE4 A:CFM2096 3.7 24.3 1.0 S4B A:CFM2096 3.7 25.4 1.0 CZ A:PHE381 4.1 19.0 1.0 S1A A:CFM2096 4.2 20.9 1.0 S2A A:CFM2096 4.3 18.7 1.0 O1 A:HCA2094 4.4 23.9 1.0 S3A A:CFM2096 4.5 23.8 1.0 O7 A:HCA2094 4.6 24.9 1.0 CG1 A:VAL70 4.6 24.6 1.0 S5 A:CFM2096 4.6 18.8 1.0 CE2 A:PHE381 4.6 21.9 1.0 FE1 A:CFM2096 5.0 21.9 1.0

Iron binding site 7 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2096 b:20.4 occ:1.00 FE7 A:CFM2096 0.0 20.4 1.0 S5 A:CFM2096 2.2 18.8 1.0 S3B A:CFM2096 2.3 23.4 1.0 FE3 A:CFM2096 2.3 22.7 1.0 S4B A:CFM2096 2.3 25.4 1.0 FE6 A:CFM2096 2.6 21.1 1.0 FE5 A:CFM2096 2.7 25.5 1.0 MO1 A:CFM2096 2.9 26.6 1.0 FE2 A:CFM2096 3.6 21.5 1.0 FE4 A:CFM2096 3.7 24.3 1.0 O A:HOH2097 3.8 14.2 1.0 S1B A:CFM2096 4.0 24.5 1.0 NE A:ARG96 4.0 27.4 1.0 S2A A:CFM2096 4.1 18.7 1.0 S4A A:CFM2096 4.2 22.6 1.0 NH2 A:ARG96 4.2 29.0 1.0 O5 A:HCA2094 4.4 26.1 1.0 S2B A:CFM2096 4.5 20.1 1.0 S3A A:CFM2096 4.5 23.8 1.0 CZ A:ARG96 4.6 29.1 1.0 NH2 A:ARG359 4.8 26.1 1.0 CZ A:ARG359 4.9 26.5 1.0 FE1 A:CFM2096 4.9 21.9 1.0 CD A:ARG96 5.0 26.0 1.0

Iron binding site 8 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2098 b:23.5 occ:1.00 FE1 B:CLF2098 0.0 23.5 1.0 S3A B:CLF2098 2.2 23.6 1.0 S2A B:CLF2098 2.3 21.4 1.0 SG B:CYS95 2.3 18.3 1.0 S1 B:CLF2098 2.3 22.6 1.0 FE2 B:CLF2098 2.6 21.9 1.0 FE4 B:CLF2098 2.7 23.2 1.0 FE3 B:CLF2098 2.8 22.1 1.0 FE8 B:CLF2098 2.9 21.8 1.0 N B:CYS95 3.3 20.0 1.0 CA B:CYS95 3.6 20.1 1.0 CB B:CYS95 3.7 17.7 1.0 OG B:SER92 3.8 36.1 1.0 S4A B:CLF2098 3.8 22.7 1.0 FE5 B:CLF2098 3.9 26.3 1.0 C B:GLY94 3.9 20.1 1.0 S4B B:CLF2098 3.9 23.7 1.0 CA B:GLY94 4.4 19.1 1.0 SG A:CYS154 4.5 23.4 1.0 SG A:CYS88 4.6 23.3 1.0 O B:GLY94 4.6 21.4 1.0 FE6 B:CLF2098 4.7 27.2 1.0 CB B:SER92 4.7 30.9 1.0 SG A:CYS62 4.8 23.1 1.0 N B:GLY94 4.8 21.5 1.0 O B:SER92 4.9 27.4 1.0

Iron binding site 9 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2098 b:21.9 occ:1.00 FE2 B:CLF2098 0.0 21.9 1.0 S4A B:CLF2098 2.3 22.7 1.0 SG A:CYS154 2.3 23.4 1.0 S1 B:CLF2098 2.3 22.6 1.0 S2A B:CLF2098 2.3 21.4 1.0 FE1 B:CLF2098 2.6 23.5 1.0 FE4 B:CLF2098 2.7 23.2 1.0 FE3 B:CLF2098 2.8 22.1 1.0 CB A:CYS154 3.7 20.1 1.0 CA A:GLY185 3.7 26.7 1.0 S3A B:CLF2098 3.7 23.6 1.0 N A:CYS154 3.8 19.0 1.0 OG B:SER92 3.9 36.1 1.0 N A:GLY185 4.1 27.0 1.0 CA A:CYS154 4.2 19.8 1.0 SG B:CYS95 4.5 18.3 1.0 FE8 B:CLF2098 4.6 21.8 1.0 FE5 B:CLF2098 4.6 26.3 1.0 C A:GLY185 4.7 27.2 1.0 SG A:CYS88 4.7 23.3 1.0 CB B:SER92 4.7 30.9 1.0 N A:PHE186 4.9 26.9 1.0 SG A:CYS62 4.9 23.1 1.0 C A:GLU153 4.9 20.0 1.0

Iron binding site 10 out of 76 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2098 b:22.1 occ:1.00 FE3 B:CLF2098 0.0 22.1 1.0 S3A B:CLF2098 2.3 23.6 1.0 SG A:CYS62 2.3 23.1 1.0 S2A B:CLF2098 2.3 21.4 1.0 S4A B:CLF2098 2.3 22.7 1.0 FE1 B:CLF2098 2.8 23.5 1.0 FE2 B:CLF2098 2.8 21.9 1.0 FE4 B:CLF2098 2.8 23.2 1.0 CB A:CYS62 3.2 23.8 1.0 CA A:GLY185 3.8 26.7 1.0 CB A:TYR64 4.0 22.1 1.0 S1 B:CLF2098 4.1 22.6 1.0 CA B:GLY94 4.2 19.1 1.0 C B:GLY94 4.4 20.1 1.0 CD2 A:TYR64 4.6 21.2 1.0 CA A:CYS62 4.6 24.2 1.0 N B:CYS95 4.6 20.0 1.0 CG A:TYR64 4.6 22.1 1.0 N A:GLY185 4.7 27.0 1.0 O B:HOH2336 4.7 26.8 1.0 C A:GLY185 4.9 27.2 1.0 SG A:CYS88 4.9 23.3 1.0 SG A:CYS154 4.9 23.4 1.0 N A:TYR64 4.9 23.6 1.0 O B:GLY94 4.9 21.4 1.0 CE2 B:TYR98 4.9 22.1 1.0 SG B:CYS95 4.9 18.3 1.0 N B:GLY94 4.9 21.5 1.0

B.Schmid, O.Einsle, H.-J.Chiu, A.Willing, M.Yoshida, J.B.Howard, D.C.Rees. Biochemical and Structural Characterization of the Crosslinked Complex of Nitrogenase: Comparison to the Adp-ALF4 Stabilized Structure Biochemistry V. 41 15557 2002.
ISSN: ISSN 0006-2960
PubMed: 12501184
DOI: 10.1021/BI026642B