Calcium in PDB 3svl: Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme

The structure of Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme, PDB code: 3svl was solved by S.Poulain, S.Eswaramoorthy, R.Hienerwadel, N.Bremond, M.D.Sylvester, Y.B.Zhang, D.Van Der Lelie, C.Berthomieu, A.C.Matin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.83 / 2.20
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.255, 107.255, 128.251, 90.00, 90.00, 120.00
R / Rfree (%)	23.7 / 27

The binding sites of Calcium atom in the Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme (pdb code 3svl). 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 Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme, PDB code: 3svl:

Calcium binding site 1 out of 1 in the Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural Basis of the Improvement of Chrr - A Multi-Purpose Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca201 b:35.2 occ:1.00 OD2 A:ASP50 2.3 14.0 1.0 O A:HOH284 2.4 24.8 1.0 O B:LEU14 2.5 15.5 1.0 O B:HOH251 2.6 13.6 1.0 OD2 A:ASP52 2.7 16.3 1.0 O A:HOH285 2.8 30.5 1.0 CG A:ASP50 3.1 14.7 1.0 OD1 A:ASP50 3.2 18.0 1.0 CG A:ASP52 3.6 16.8 1.0 C B:LEU14 3.6 13.5 1.0 CB A:ASP52 3.8 16.4 1.0 CA B:ARG15 3.9 14.1 1.0 N B:LYS16 4.1 15.2 1.0 N B:ARG15 4.2 13.0 1.0 C B:ARG15 4.4 13.9 1.0 CB A:ASP50 4.5 13.3 1.0 CB B:LEU14 4.7 14.7 1.0 OD1 A:ASP52 4.7 16.3 1.0 CA B:LEU14 4.7 14.2 1.0 CB B:ARG15 4.9 13.7 1.0

S.Eswaramoorthy, S.Poulain, R.Hienerwadel, N.Bremond, M.D.Sylvester, Y.B.Zhang, C.Berthomieu, D.Van Der Lelie, A.Matin. Crystal Structure of Chrr-A Quinone Reductase with the Capacity to Reduce Chromate. Plos One V. 7 36017 2012.
ISSN: ESSN 1932-6203
PubMed: 22558308
DOI: 10.1371/JOURNAL.PONE.0036017