Calcium in PDB 1l5h: Femo-Cofactor Deficient Nitrogenase Mofe Protein

All present enzymatic activity of Femo-Cofactor Deficient Nitrogenase Mofe Protein:
1.18.6.1;

The structure of Femo-Cofactor Deficient Nitrogenase Mofe Protein, PDB code: 1l5h was solved by B.Schmid, M.W.Ribbe, O.Einsle, M.Yoshida, L.M.Thomas, D.R.Dean, D.C.Rees, B.K.Burgess, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	150.452, 191.922, 102.339, 90.00, 90.00, 90.00
R / Rfree (%)	24.9 / 28.9

The structure of Femo-Cofactor Deficient Nitrogenase Mofe Protein also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Calcium atom in the Femo-Cofactor Deficient Nitrogenase Mofe Protein (pdb code 1l5h). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Femo-Cofactor Deficient Nitrogenase Mofe Protein, PDB code: 1l5h:

Calcium binding site 1 out of 1 in the Femo-Cofactor Deficient Nitrogenase Mofe Protein


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Femo-Cofactor Deficient Nitrogenase Mofe Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca601 b:45.2 occ:1.00 O B:ARG108 2.4 43.2 1.0 O B:HOH708 2.4 50.2 1.0 O A:HOH549 2.4 53.2 1.0 OE1 B:GLU109 2.6 56.2 1.0 CD B:GLU109 2.7 54.8 1.0 OE2 B:GLU109 2.8 56.8 1.0 C B:ARG108 3.6 43.4 1.0 CG B:GLU109 3.7 51.4 1.0 NZ A:LYS433 4.1 50.4 1.0 CA B:GLU109 4.3 46.0 1.0 CB B:ARG108 4.4 44.5 1.0 N B:GLU109 4.4 44.4 1.0 O B:HOH640 4.5 43.5 1.0 O B:PHE107 4.5 39.7 1.0 CB B:GLU109 4.5 46.0 1.0 CA B:ARG108 4.6 42.8 1.0 CE A:LYS433 4.7 50.1 1.0 O B:HOH664 4.8 40.1 1.0 O A:HOH547 4.8 46.2 1.0 O B:HOH751 4.9 42.7 1.0

B.Schmid, M.W.Ribbe, O.Einsle, M.Yoshida, L.M.Thomas, D.R.Dean, D.C.Rees, B.K.Burgess. Structure of A Cofactor-Deficient Nitrogenase Mofe Protein. Science V. 296 352 2002.
ISSN: ISSN 0036-8075
PubMed: 11951047
DOI: 10.1126/SCIENCE.1070010