Calcium in PDB 3eu3: Crystal Structure of Bdbd From Bacillus Subtilis (Reduced)

The structure of Crystal Structure of Bdbd From Bacillus Subtilis (Reduced), PDB code: 3eu3 was solved by A.Crow, M.C.Moller, L.Hederstedt, N.E.Le Brun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.08 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.774, 43.399, 54.658, 90.00, 107.40, 90.00
R / Rfree (%)	18.6 / 21.9

The binding sites of Calcium atom in the Crystal Structure of Bdbd From Bacillus Subtilis (Reduced) (pdb code 3eu3). 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 Crystal Structure of Bdbd From Bacillus Subtilis (Reduced), PDB code: 3eu3:

Calcium binding site 1 out of 1 in the Crystal Structure of Bdbd From Bacillus Subtilis (Reduced)


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 Bdbd From Bacillus Subtilis (Reduced) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1 b:13.6 occ:1.00 OE2 A:GLU115 2.3 18.1 1.0 OE1 A:GLN49 2.3 11.1 1.0 O A:HOH234 2.4 14.2 1.0 O A:HOH232 2.4 12.8 1.0 OD2 A:ASP180 2.5 13.6 1.0 OD1 A:ASP180 2.6 15.1 1.0 O A:HOH233 2.6 16.1 1.0 CG A:ASP180 2.8 14.2 1.0 CD A:GLU115 3.3 16.4 1.0 CD A:GLN49 3.3 11.3 1.0 OE1 A:GLU115 3.6 17.2 1.0 NE2 A:GLN49 3.7 11.9 1.0 ND2 A:ASN99 4.0 16.9 1.0 CD A:PRO50 4.2 12.7 1.0 O A:GLN176 4.3 15.8 1.0 CB A:ASP180 4.3 14.3 1.0 O A:HOH314 4.4 21.6 1.0 CG A:GLU115 4.6 15.6 1.0 O A:PHE97 4.6 9.9 1.0 O A:GLY48 4.7 13.7 1.0 CG A:GLN49 4.7 10.6 1.0 CA A:GLN49 4.7 11.7 1.0 N A:ASN99 4.8 11.7 1.0 CA A:VAL98 4.9 10.2 1.0 CB A:GLN49 4.9 11.1 1.0 OE1 A:GLN176 5.0 19.4 1.0

A.Crow, A.Lewin, O.Hecht, M.Carlsson Moller, G.R.Moore, L.Hederstedt, N.E.Le Brun. Crystal Structure and Biophysical Properties of Bacillus Subtilis Bdbd: An Oxidizing Thiol:Disulfide Oxidoreductase Containing A Novel Metal Site J.Biol.Chem. V. 284 23719 2009.
ISSN: ISSN 0021-9258
PubMed: 19535335
DOI: 10.1074/JBC.M109.005785