Molybdenum in PDB 1qh1: Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State

All present enzymatic activity of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State:
1.18.6.1;

The structure of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State, PDB code: 1qh1 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 (°)	204.180, 75.220, 162.840, 90.00, 122.88, 90.00
R / Rfree (%)	15.8 / 19.9

The structure of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized 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 Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State (pdb code 1qh1). 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 Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State, PDB code: 1qh1:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo503 b:14.4 occ:1.00 MO1 A:CFM503 0.0 14.4 1.0 S1B A:CFM503 2.3 12.6 1.0 O5 A:HCA501 2.3 11.7 1.0 S4B A:CFM503 2.4 11.8 1.0 S3B A:CFM503 2.4 13.3 1.0 O7 A:HCA501 2.4 13.7 1.0 ND1 A:HIS440 2.4 14.3 1.0 FE6 A:CFM503 2.7 14.1 1.0 FE7 A:CFM503 2.7 13.6 1.0 FE5 A:CFM503 2.7 13.9 1.0 C7 A:HCA501 3.1 16.1 1.0 CE1 A:HIS440 3.3 14.0 1.0 C3 A:HCA501 3.3 15.9 1.0 CG A:HIS440 3.4 11.2 1.0 CB A:HIS440 3.7 13.7 1.0 C2 A:HCA501 4.1 13.2 1.0 O2 A:HCA501 4.1 15.5 1.0 O A:HOH3012 4.2 14.1 1.0 O6 A:HCA501 4.2 13.0 1.0 C5 A:HCA501 4.2 13.5 1.0 C4 A:HCA501 4.3 14.6 1.0 NE2 A:HIS440 4.4 13.5 1.0 CD2 A:HIS440 4.5 10.5 1.0 CA A:HIS440 4.6 12.8 1.0 C1 A:HCA501 4.8 15.5 1.0 S2B A:CFM503 4.8 13.3 1.0 S5 A:CFM503 4.8 12.4 1.0 S3A A:CFM503 4.9 12.3 1.0

Molybdenum binding site 2 out of 2 in the Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofe Protein From Klebsiella Pneumoniae, Phenosafranin Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo503 b:15.1 occ:1.00 MO1 C:CFM503 0.0 15.1 1.0 O5 C:HCA501 2.3 12.7 1.0 O7 C:HCA501 2.3 14.7 1.0 S4B C:CFM503 2.3 12.2 1.0 S1B C:CFM503 2.3 13.4 1.0 S3B C:CFM503 2.4 13.7 1.0 ND1 C:HIS440 2.5 14.8 1.0 FE6 C:CFM503 2.7 14.3 1.0 FE7 C:CFM503 2.7 13.6 1.0 FE5 C:CFM503 2.7 14.7 1.0 C7 C:HCA501 3.1 16.7 1.0 C3 C:HCA501 3.3 14.1 1.0 CE1 C:HIS440 3.4 13.0 1.0 CG C:HIS440 3.5 14.0 1.0 CB C:HIS440 3.8 14.2 1.0 O2 C:HCA501 4.2 14.4 1.0 C2 C:HCA501 4.2 14.3 1.0 C5 C:HCA501 4.2 12.7 1.0 O C:HOH1335 4.2 15.5 1.0 O6 C:HCA501 4.2 13.7 1.0 C4 C:HCA501 4.3 12.7 1.0 NE2 C:HIS440 4.5 14.2 1.0 CD2 C:HIS440 4.6 14.3 1.0 CA C:HIS440 4.7 12.3 1.0 S5 C:CFM503 4.7 13.1 1.0 S2B C:CFM503 4.8 13.6 1.0 C1 C:HCA501 4.8 14.8 1.0 S3A C:CFM503 4.9 14.1 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