Calcium in PDB 6gaq: Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus

The structure of Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus, PDB code: 6gaq was solved by M.Lofstad, I.Gudim, H.-P.Hersleth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.73 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	101.010, 125.451, 59.260, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 29.3

The structure of Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus (pdb code 6gaq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus, PDB code: 6gaq:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus


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 Oxidised Flavodoxin 2 From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1002 b:35.8 occ:1.00 OE1 A:GLU138 2.5 38.4 1.0 O A:HOH1103 2.5 25.0 1.0 OD2 A:ASP136 2.6 48.5 1.0 CG A:GLU138 3.2 48.1 1.0 CD A:GLU138 3.3 53.5 1.0 CG A:ASP136 3.6 45.9 1.0 OD1 A:ASP136 3.9 38.2 1.0 OE2 A:GLU138 4.5 42.0 1.0 CB A:GLU138 4.7 51.2 1.0 O A:HOH1105 4.8 25.0 1.0 CB A:ASP136 4.8 16.9 1.0 OD2 A:ASP139 4.9 35.0 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus


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 Oxidised Flavodoxin 2 From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1003 b:29.8 occ:1.00 OD1 A:ASP139 2.4 20.8 1.0 O A:ALA133 2.4 35.5 1.0 O A:HOH1104 2.5 26.1 1.0 O A:GLU131 2.5 34.0 1.0 CG A:ASP139 3.4 30.6 1.0 C A:ALA133 3.6 29.1 1.0 C A:GLU131 3.7 32.2 1.0 OD2 A:ASP139 4.0 35.0 1.0 OD1 A:ASP136 4.1 38.2 1.0 N A:ALA133 4.2 23.5 1.0 N A:GLU135 4.4 20.2 1.0 CA A:PRO134 4.4 31.2 1.0 N A:PRO134 4.4 29.7 1.0 C A:LEU132 4.4 34.4 1.0 CB A:ASP139 4.4 20.2 1.0 CG2 A:ILE130 4.5 33.3 1.0 CA A:ALA133 4.5 35.5 1.0 CA A:GLU131 4.5 39.2 1.0 N A:GLU131 4.6 29.2 1.0 CB A:LEU132 4.6 21.2 1.0 N A:LEU132 4.7 29.9 1.0 CB A:GLU131 4.7 24.4 1.0 CG A:GLU135 4.7 14.8 1.0 CA A:LEU132 4.8 36.5 1.0 O A:LEU132 4.8 30.2 1.0 C A:PRO134 4.9 40.5 1.0 CG A:GLU131 4.9 27.4 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Oxidised Flavodoxin 2 From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1003 b:30.2 occ:1.00 O B:GLU131 2.4 22.1 1.0 OD2 B:ASP139 2.4 17.5 1.0 O B:HOH1102 2.4 19.8 0.5 O B:HOH1107 2.4 17.0 0.5 O B:ALA133 2.5 37.2 1.0 CG B:ASP139 3.5 30.0 1.0 C B:ALA133 3.6 21.4 1.0 C B:GLU131 3.6 32.3 1.0 OD1 B:ASP136 4.1 41.0 1.0 N B:ALA133 4.1 28.3 1.0 OD1 B:ASP139 4.2 34.5 1.0 C B:LEU132 4.4 31.0 1.0 CG2 B:ILE130 4.4 29.0 1.0 N B:PRO134 4.4 38.3 1.0 CA B:PRO134 4.4 30.2 1.0 CA B:GLU131 4.4 35.0 1.0 N B:GLU135 4.4 39.3 1.0 CA B:ALA133 4.4 37.6 1.0 CB B:GLU131 4.5 22.0 1.0 CB B:ASP139 4.5 19.9 1.0 N B:GLU131 4.5 28.4 1.0 N B:LEU132 4.6 34.0 1.0 CB B:LEU132 4.7 22.0 1.0 CA B:LEU132 4.8 23.8 1.0 CG B:GLU131 4.8 25.9 1.0 O B:LEU132 4.8 28.9 1.0 CG B:GLU135 4.9 25.6 1.0 O B:HOH1104 5.0 27.4 1.0 OE1 B:GLU135 5.0 48.1 1.0 C B:PRO134 5.0 45.9 1.0

I.Gudim, M.Hammerstad, M.Lofstad, H.P.Hersleth. The Characterization of Different Flavodoxin Reductase-Flavodoxin (Fnr-Fld) Interactions Reveals An Efficient Fnr-Fld Redox Pair and Identifies A Novel Fnr Subclass. Biochemistry V. 57 5427 2018.
ISSN: ISSN 1520-4995
PubMed: 30142264
DOI: 10.1021/ACS.BIOCHEM.8B00674