Molybdenum in PDB 4tku: Reactivated Nitrogenase Mofe-Protein From A. Vinelandii

All present enzymatic activity of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii:
1.18.6.1;

The structure of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tku was solved by T.Spatzal, K.Perez, O.Einsle, 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)	38.65 / 1.43
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.941, 130.785, 107.005, 90.00, 110.58, 90.00
R / Rfree (%)	13.2 / 14.2

The structure of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii also contains other interesting chemical elements:

Iron	(Fe)	32 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Molybdenum atom in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii (pdb code 4tku). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tku:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:8.1 occ:1.00 MO1 A:ICS502 0.0 8.1 1.0 O5 A:HCA501 2.2 8.0 1.0 O7 A:HCA501 2.2 7.7 1.0 S4B A:ICS502 2.3 8.2 1.0 S1B A:ICS502 2.3 8.4 1.0 S3B A:ICS502 2.4 8.1 1.0 ND1 A:HIS442 2.4 7.8 1.0 FE6 A:ICS502 2.7 8.2 1.0 FE7 A:ICS502 2.7 8.1 1.0 FE5 A:ICS502 2.7 8.5 1.0 C7 A:HCA501 3.1 7.5 1.0 C3 A:HCA501 3.2 7.3 1.0 CE1 A:HIS442 3.2 8.3 1.0 CG A:HIS442 3.4 7.7 1.0 CX A:ICS502 3.5 8.3 1.0 CB A:HIS442 3.8 7.6 1.0 C2 A:HCA501 4.1 6.9 1.0 O A:HOH643 4.2 10.6 1.0 C5 A:HCA501 4.2 8.4 1.0 O6 A:HCA501 4.2 8.2 1.0 C4 A:HCA501 4.3 8.5 1.0 O1 A:HCA501 4.3 10.0 1.0 NE2 A:HIS442 4.4 7.7 1.0 CD2 A:HIS442 4.5 7.2 1.0 CA A:HIS442 4.6 7.3 1.0 S2B A:ICS502 4.8 8.8 1.0 C1 A:HCA501 4.8 8.6 1.0 S5A A:ICS502 4.8 8.6 1.0 S3A A:ICS502 4.9 8.8 1.0

Molybdenum binding site 2 out of 2 in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:8.2 occ:1.00 MO1 C:ICS502 0.0 8.2 1.0 O5 C:HCA501 2.2 7.0 1.0 O7 C:HCA501 2.2 7.4 1.0 S4B C:ICS502 2.3 8.4 1.0 S1B C:ICS502 2.3 8.3 1.0 S3B C:ICS502 2.4 8.4 1.0 ND1 C:HIS442 2.4 8.3 1.0 FE6 C:ICS502 2.7 8.3 1.0 FE7 C:ICS502 2.7 8.2 1.0 FE5 C:ICS502 2.7 8.5 1.0 C7 C:HCA501 3.0 7.2 1.0 C3 C:HCA501 3.2 7.4 1.0 CE1 C:HIS442 3.3 8.1 1.0 CG C:HIS442 3.4 7.4 1.0 CX C:ICS502 3.5 8.1 1.0 CB C:HIS442 3.7 8.0 1.0 C2 C:HCA501 4.2 7.5 1.0 O C:HOH645 4.2 9.8 1.0 O6 C:HCA501 4.2 8.5 1.0 C5 C:HCA501 4.3 7.3 1.0 C4 C:HCA501 4.3 8.2 1.0 O1 C:HCA501 4.4 9.7 1.0 NE2 C:HIS442 4.4 7.8 1.0 CD2 C:HIS442 4.5 8.0 1.0 CA C:HIS442 4.6 7.8 1.0 S2B C:ICS502 4.7 8.3 1.0 S5A C:ICS502 4.8 8.5 1.0 C1 C:HCA501 4.8 8.9 1.0 S3A C:ICS502 4.9 8.8 1.0

T.Spatzal, K.A.Perez, O.Einsle, J.B.Howard, D.C.Rees. Ligand Binding to the Femo-Cofactor: Structures of Co-Bound and Reactivated Nitrogenase. Science V. 345 1620 2014.
ISSN: ESSN 1095-9203
PubMed: 25258081
DOI: 10.1126/SCIENCE.1256679