Calcium in PDB 2fi1: The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4

The structure of The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4, PDB code: 2fi1 was solved by R.Zhang, M.Zhou, J.Abdullah, F.Collart, A.Joachimiak, Midwest Center Forstructural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.00 / 1.40
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	71.417, 71.417, 104.790, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 17

The binding sites of Calcium atom in the The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4 (pdb code 2fi1). 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 The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4, PDB code: 2fi1:

Calcium binding site 1 out of 1 in the The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca191 b:10.9 occ:1.00 O A:GLY14 2.3 10.2 1.0 O A:HOH242 2.3 14.9 1.0 OD1 A:ASP160 2.4 10.9 1.0 O A:HOH209 2.4 12.1 1.0 OD2 A:ASP12 2.4 11.1 1.0 O A:HOH253 2.4 15.0 1.0 OD1 A:ASP12 2.8 11.4 1.0 CG A:ASP12 2.9 10.7 1.0 CG A:ASP160 3.4 9.9 1.0 C A:GLY14 3.5 9.6 1.0 OD2 A:ASP160 3.8 13.4 1.0 O A:HOH526 3.8 45.1 1.0 OD2 A:ASP164 4.2 10.8 1.0 O A:HOH259 4.3 17.7 1.0 CA A:GLY14 4.3 10.1 1.0 O A:HOH273 4.3 18.9 1.0 CB A:ASP12 4.4 8.7 1.0 N A:GLY15 4.4 9.3 1.0 N A:GLY14 4.4 9.8 1.0 O A:HOH389 4.5 29.5 1.0 CA A:GLY15 4.6 9.2 1.0 N A:ASP160 4.6 8.0 1.0 CD A:ARG161 4.6 16.2 1.0 OG1 A:THR16 4.7 10.0 1.0 CB A:ASP160 4.7 8.6 1.0 CG A:ARG161 4.7 12.8 1.0 C A:GLY15 5.0 9.2 1.0

R.Zhang, M.Zhou, J.Abdullah, F.Collart, A.Joachimiak. The 1.4A Crystal Structure of A Hydrolase From Streptococcus Pneumoniae TIGR4 To Be Published.