Calcium in PDB 3tew: Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution

The structure of Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution, PDB code: 3tew was solved by G.K.Feld, B.A.Krantz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.355, 93.385, 118.078, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 21.6

The binding sites of Calcium atom in the Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution (pdb code 3tew). 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 Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution, PDB code: 3tew:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution


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 Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca800 b:8.9 occ:1.00 O A:ILE183 2.3 11.2 1.0 OD1 A:ASP177 2.3 14.0 1.0 OD1 A:ASP179 2.4 10.9 1.0 OD1 A:ASP181 2.4 8.6 1.0 OE2 A:GLU188 2.4 10.3 1.0 O A:HOH802 2.4 14.3 1.0 CG A:ASP181 3.2 7.3 1.0 CG A:ASP179 3.3 10.9 1.0 C A:ILE183 3.5 9.9 1.0 CD A:GLU188 3.5 8.5 1.0 OD2 A:ASP181 3.5 8.5 1.0 CG A:ASP177 3.6 17.1 1.0 OD2 A:ASP179 3.6 11.1 1.0 N A:ILE183 3.8 10.8 1.0 CA A:ILE183 4.1 11.0 1.0 N A:ASP181 4.2 9.6 1.0 CA A:CA801 4.2 7.3 1.0 CB A:ILE183 4.2 10.5 1.0 CG A:GLU188 4.3 9.4 1.0 CA A:ASP177 4.3 17.2 1.0 OD2 A:ASP177 4.3 18.3 1.0 O A:PRO223 4.3 11.8 1.0 OE1 A:GLU188 4.4 9.7 1.0 N A:GLY182 4.5 11.5 1.0 CB A:ASP181 4.5 8.7 1.0 CB A:ASP177 4.5 17.8 1.0 N A:ASP179 4.5 13.9 1.0 C A:PRO184 4.6 12.8 1.0 N A:PRO184 4.6 11.3 1.0 C A:ASP177 4.6 18.5 1.0 CA A:PRO223 4.6 10.5 1.0 OD1 A:ASP185 4.6 22.4 1.0 CA A:ASP181 4.7 8.2 1.0 CB A:ASP179 4.7 9.7 1.0 N A:ASP185 4.7 14.4 1.0 N A:ASN180 4.7 10.8 1.0 C A:GLY182 4.8 11.5 1.0 N A:ARG178 4.8 17.1 1.0 O A:PRO184 4.8 13.0 1.0 CA A:PRO184 4.8 12.8 1.0 C A:PRO223 4.8 10.2 1.0 C A:ASP181 4.9 10.4 1.0 CA A:ASP179 4.9 11.1 1.0 C A:ASP179 5.0 9.9 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution


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 Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca801 b:7.3 occ:1.00 OD2 A:ASP181 2.3 8.5 1.0 OD2 A:ASP179 2.3 11.1 1.0 O A:SER222 2.3 9.7 1.0 OD2 A:ASP235 2.4 8.1 1.0 O A:LYS225 2.4 7.2 1.0 OE1 A:GLU188 2.5 9.7 1.0 OE2 A:GLU188 2.9 10.3 1.0 CD A:GLU188 3.1 8.5 1.0 CG A:ASP179 3.4 10.9 1.0 CG A:ASP181 3.4 7.3 1.0 CG A:ASP235 3.5 8.8 1.0 C A:LYS225 3.5 6.3 1.0 C A:SER222 3.5 10.3 1.0 OD1 A:ASP179 3.9 10.9 1.0 CB A:ASP235 4.0 8.4 1.0 OG1 A:THR228 4.0 7.1 1.0 OD1 A:ASP181 4.1 8.6 1.0 O A:TRP226 4.1 7.8 1.0 CA A:CA800 4.2 8.9 1.0 CA A:PRO223 4.3 10.5 1.0 N A:TRP226 4.3 6.5 1.0 N A:LYS225 4.3 8.6 1.0 CA A:TRP226 4.3 7.3 1.0 C A:TRP226 4.3 6.8 1.0 N A:PRO223 4.4 9.9 1.0 CA A:LYS225 4.4 7.9 1.0 N A:SER222 4.5 7.2 1.0 C A:PRO223 4.5 10.2 1.0 OD1 A:ASP235 4.5 8.0 1.0 CB A:ASP181 4.5 8.7 1.0 CG A:GLU188 4.5 9.4 1.0 OG A:SER221 4.6 10.3 1.0 CA A:SER222 4.6 9.2 1.0 CB A:ASP179 4.6 9.7 1.0 CB A:SER221 4.7 8.5 1.0 N A:GLU224 4.8 9.7 1.0 O A:PRO223 4.9 11.8 1.0

G.K.Feld, A.F.Kintzer, I.I.Tang, K.L.Thoren, B.A.Krantz. Domain Flexibility Modulates the Heterogeneous Assembly Mechanism of Anthrax Toxin Protective Antigen. J.Mol.Biol. V. 415 159 2012.
ISSN: ISSN 0022-2836
PubMed: 22063095
DOI: 10.1016/J.JMB.2011.10.035