Molybdenum in PDB 4tkv: Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii

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

The structure of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tkv 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)	38.74 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.172, 130.623, 106.996, 90.00, 110.65, 90.00
R / Rfree (%)	13.8 / 15.4

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

Iron

(Fe)

32 atoms

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

Molybdenum binding site 1 out of 2 in the Co-Bound 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 Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:11.4 occ:1.00 MO1 A:ICE502 0.0 11.4 1.0 O6 A:HCA501 2.2 11.1 1.0 O7 A:HCA501 2.2 12.2 1.0 S1B A:ICE502 2.3 11.2 1.0 S4B A:ICE502 2.3 11.9 1.0 S3B A:ICE502 2.4 11.9 1.0 ND1 A:HIS442 2.4 11.9 1.0 FE6 A:ICE502 2.6 11.6 1.0 FE7 A:ICE502 2.7 11.7 1.0 FE5 A:ICE502 2.7 11.9 1.0 C7 A:HCA501 3.0 11.5 1.0 C3 A:HCA501 3.2 10.7 1.0 CE1 A:HIS442 3.3 10.6 1.0 CG A:HIS442 3.4 10.9 1.0 CX A:ICE502 3.5 11.7 1.0 CB A:HIS442 3.7 11.1 1.0 C2 A:HCA501 4.1 11.1 1.0 O A:HOH657 4.2 13.9 1.0 O5 A:HCA501 4.2 11.4 1.0 C4 A:HCA501 4.3 10.5 1.0 C5 A:HCA501 4.3 10.7 1.0 O2 A:HCA501 4.4 14.2 1.0 C A:CMO504 4.4 11.8 1.0 NE2 A:HIS442 4.4 11.9 1.0 CD2 A:HIS442 4.5 11.1 1.0 CA A:HIS442 4.5 10.6 1.0 S5A A:ICE502 4.8 11.7 1.0 C1 A:HCA501 4.8 12.2 1.0 FE2 A:ICE502 4.9 11.7 1.0 S3A A:ICE502 4.9 12.2 1.0

Molybdenum binding site 2 out of 2 in the Co-Bound 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 Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:11.7 occ:1.00 MO1 C:ICE502 0.0 11.7 1.0 O7 C:HCA501 2.2 10.6 1.0 O5 C:HCA501 2.2 11.7 1.0 S4B C:ICE502 2.3 11.8 1.0 S1B C:ICE502 2.3 11.6 1.0 S3B C:ICE502 2.3 12.0 1.0 ND1 C:HIS442 2.4 11.2 1.0 FE6 C:ICE502 2.6 11.8 1.0 FE7 C:ICE502 2.7 11.6 1.0 FE5 C:ICE502 2.7 12.4 1.0 C7 C:HCA501 3.0 11.3 1.0 C3 C:HCA501 3.2 11.0 1.0 CE1 C:HIS442 3.3 10.1 1.0 CG C:HIS442 3.4 11.0 1.0 CX C:ICE502 3.5 11.3 1.0 CB C:HIS442 3.7 11.1 1.0 C2 C:HCA501 4.1 11.5 1.0 O6 C:HCA501 4.2 11.7 1.0 O C:HOH645 4.2 13.1 1.0 C5 C:HCA501 4.3 9.7 1.0 C4 C:HCA501 4.3 10.0 1.0 C C:CMO504 4.4 10.4 1.0 O1 C:HCA501 4.4 13.7 1.0 NE2 C:HIS442 4.4 10.6 1.0 CD2 C:HIS442 4.5 11.0 1.0 CA C:HIS442 4.6 10.7 1.0 S5A C:ICE502 4.8 12.2 1.0 C1 C:HCA501 4.8 12.8 1.0 FE2 C:ICE502 4.9 11.7 1.0 S3A C:ICE502 4.9 11.8 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