Calcium in PDB 1fp4: Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase

All present enzymatic activity of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase:
1.18.6.1;

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4 was solved by M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	107.200, 130.200, 80.400, 90.00, 111.20, 90.00
R / Rfree (%)	18.4 / 24

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	30 atoms

The binding sites of Calcium atom in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase (pdb code 1fp4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca524 b:14.4 occ:1.00 O D:ARG108 2.3 19.8 1.0 OD2 B:ASP357 2.5 18.4 1.0 OE1 D:GLU109 2.6 22.8 1.0 OD2 B:ASP353 2.8 34.9 1.0 OD1 B:ASP353 2.9 27.9 1.0 OD1 B:ASP357 3.1 18.6 1.0 CG B:ASP357 3.1 15.9 1.0 CG B:ASP353 3.2 28.6 1.0 CD D:GLU109 3.4 28.6 1.0 NZ C:LYS433 3.4 28.5 1.0 C D:ARG108 3.5 16.4 1.0 CG D:GLU109 3.7 27.4 1.0 CA D:GLU109 4.1 18.1 1.0 N D:GLU109 4.2 15.3 1.0 CB D:ARG108 4.3 13.3 1.0 O D:PHE107 4.4 14.3 1.0 CB D:GLU109 4.5 21.6 1.0 OE2 D:GLU109 4.5 37.1 1.0 CD2 C:PHE429 4.5 11.3 1.0 CA D:ARG108 4.5 12.3 1.0 O B:ASP353 4.6 17.3 1.0 CB B:ASP357 4.6 18.0 1.0 CB B:ASP353 4.7 23.7 1.0 CE C:LYS433 4.7 22.8 1.0 C B:ASP353 5.0 17.1 1.0 CG C:PHE429 5.0 12.3 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca524 b:13.4 occ:1.00 O B:ARG108 2.3 18.0 1.0 OD2 D:ASP357 2.5 19.1 1.0 OE1 B:GLU109 2.6 23.1 1.0 OD2 D:ASP353 2.6 36.1 1.0 OD1 D:ASP353 2.8 26.4 1.0 CG D:ASP353 3.1 28.1 1.0 OD1 D:ASP357 3.2 17.9 1.0 CG D:ASP357 3.2 16.7 1.0 CD B:GLU109 3.5 28.3 1.0 C B:ARG108 3.5 16.7 1.0 NZ A:LYS433 3.6 27.0 1.0 CG B:GLU109 3.7 28.2 1.0 CA B:GLU109 4.2 18.2 1.0 N B:GLU109 4.2 14.6 1.0 CB B:ARG108 4.3 14.2 1.0 O B:PHE107 4.4 14.4 1.0 CD2 A:PHE429 4.4 11.0 1.0 CB B:GLU109 4.5 22.8 1.0 CA B:ARG108 4.5 13.8 1.0 OE2 B:GLU109 4.5 35.3 1.0 CB D:ASP353 4.6 21.9 1.0 O D:ASP353 4.6 18.1 1.0 CB D:ASP357 4.7 18.1 1.0 CE A:LYS433 4.9 20.8 1.0 CG A:PHE429 4.9 11.2 1.0 C D:ASP353 4.9 17.4 1.0 O B:HOH554 4.9 26.6 1.0 CE2 A:PHE429 5.0 10.2 1.0

M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales. Mechanistic Features and Structure of the Nitrogenase Alpha-GLN195 Mofe Protein Biochemistry V. 40 1540 2001.
ISSN: ISSN 0006-2960
PubMed: 11327812
DOI: 10.1021/BI0013997