Molybdenum in PDB 1qgu: Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State

All present enzymatic activity of Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State:
1.18.6.1;

The structure of Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State, PDB code: 1qgu was solved by S.M.Mayer, D.M.Lawson, C.A.Gormal, S.M.Roe, B.E.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	204.030, 75.300, 163.010, 90.00, 122.61, 90.00
R / Rfree (%)	15.6 / 19.9

The structure of Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State also contains other interesting chemical elements:

Magnesium	(Mg)	7 atoms
Iron	(Fe)	30 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Molybdenum atom in the Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State (pdb code 1qgu). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State, PDB code: 1qgu:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo503 b:10.9 occ:1.00 MO1 A:CFM503 0.0 10.9 1.0 O5 A:HCA501 2.3 8.7 1.0 S1B A:CFM503 2.3 9.1 1.0 S4B A:CFM503 2.3 8.8 1.0 O7 A:HCA501 2.4 10.1 1.0 S3B A:CFM503 2.4 9.3 1.0 ND1 A:HIS440 2.5 11.7 1.0 FE7 A:CFM503 2.7 9.6 1.0 FE6 A:CFM503 2.7 10.0 1.0 FE5 A:CFM503 2.7 10.3 1.0 C7 A:HCA501 3.1 11.8 1.0 CE1 A:HIS440 3.3 10.4 1.0 C3 A:HCA501 3.4 10.3 1.0 CG A:HIS440 3.4 9.1 1.0 CB A:HIS440 3.8 10.4 1.0 C2 A:HCA501 4.1 10.1 1.0 O A:HOH3009 4.2 10.4 1.0 C5 A:HCA501 4.2 10.7 1.0 O6 A:HCA501 4.2 10.4 1.0 O2 A:HCA501 4.3 13.9 1.0 C4 A:HCA501 4.3 9.7 1.0 NE2 A:HIS440 4.5 9.3 1.0 CD2 A:HIS440 4.5 8.5 1.0 CA A:HIS440 4.7 9.6 1.0 S2B A:CFM503 4.8 10.1 1.0 S5 A:CFM503 4.8 8.8 1.0 C1 A:HCA501 4.8 12.1 1.0 S3A A:CFM503 4.9 8.9 1.0

Molybdenum binding site 2 out of 2 in the Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mo-Fe Protein From Klebsiella Pneumoniae, Dithionite-Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo503 b:12.3 occ:1.00 MO1 C:CFM503 0.0 12.3 1.0 O5 C:HCA501 2.3 8.7 1.0 S4B C:CFM503 2.3 10.3 1.0 S1B C:CFM503 2.3 10.1 1.0 O7 C:HCA501 2.4 10.3 1.0 S3B C:CFM503 2.4 10.0 1.0 ND1 C:HIS440 2.5 11.2 1.0 FE7 C:CFM503 2.7 11.3 1.0 FE6 C:CFM503 2.7 11.4 1.0 FE5 C:CFM503 2.7 11.9 1.0 C7 C:HCA501 3.1 13.2 1.0 C3 C:HCA501 3.3 9.4 1.0 CE1 C:HIS440 3.4 11.3 1.0 CG C:HIS440 3.5 9.3 1.0 CB C:HIS440 3.7 16.0 1.0 C5 C:HCA501 4.2 10.0 1.0 C2 C:HCA501 4.2 9.9 1.0 O C:HOH1396 4.2 12.4 1.0 O6 C:HCA501 4.2 10.3 1.0 C4 C:HCA501 4.3 9.5 1.0 O2 C:HCA501 4.3 14.4 1.0 NE2 C:HIS440 4.5 11.6 1.0 CD2 C:HIS440 4.6 11.3 1.0 CA C:HIS440 4.6 10.8 1.0 S5 C:CFM503 4.8 10.5 1.0 S2B C:CFM503 4.8 10.8 1.0 C1 C:HCA501 4.9 10.9 1.0 S3A C:CFM503 4.9 10.9 1.0

S.M.Mayer, D.M.Lawson, C.A.Gormal, S.M.Roe, B.E.Smith. New Insights Into Structure-Function Relationships in Nitrogenase: A 1.6 A Resolution X-Ray Crystallographic Study of Klebsiella Pneumoniae Mofe-Protein. J.Mol.Biol. V. 292 871 1999.
ISSN: ISSN 0022-2836
PubMed: 10525412
DOI: 10.1006/JMBI.1999.3107