Calcium in PDB 3tex: Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.7-A Resolution

The structure of Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.7-A Resolution, PDB code: 3tex 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)	9.99 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.396, 93.937, 117.848, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 21.7

The binding sites of Calcium atom in the Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.7-A Resolution (pdb code 3tex). 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 1.7-A Resolution, PDB code: 3tex:
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 1.7-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 1.7-A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca800 b:27.5 occ:1.00 O A:ILE183 2.3 29.2 1.0 OE2 A:GLU188 2.3 27.6 1.0 OD1 A:ASP177 2.4 28.0 1.0 OD1 A:ASP179 2.4 28.6 1.0 OD1 A:ASP181 2.5 28.4 1.0 O A:HOH802 2.5 30.8 1.0 CG A:ASP181 3.3 28.2 1.0 CG A:ASP179 3.3 30.0 1.0 C A:ILE183 3.4 28.5 1.0 CD A:GLU188 3.5 28.8 1.0 CG A:ASP177 3.6 30.8 1.0 OD2 A:ASP179 3.6 29.9 1.0 OD2 A:ASP181 3.6 25.8 1.0 N A:ILE183 3.8 28.6 1.0 CA A:ILE183 4.0 28.1 1.0 N A:ASP181 4.2 26.2 1.0 CB A:ILE183 4.2 26.2 1.0 CA A:ASP177 4.3 28.6 1.0 CG A:GLU188 4.3 27.3 1.0 CA A:CA801 4.3 26.4 1.0 O A:PRO223 4.3 28.9 1.0 OD2 A:ASP177 4.4 31.9 1.0 OE1 A:GLU188 4.4 29.5 1.0 CB A:ASP177 4.5 29.8 1.0 N A:GLY182 4.5 30.1 1.0 CB A:ASP181 4.5 25.0 1.0 C A:ASP177 4.5 27.9 1.0 N A:ASP179 4.5 30.1 1.0 N A:PRO184 4.6 31.3 1.0 C A:PRO184 4.6 29.4 1.0 N A:ASP185 4.6 30.7 1.0 OD1 A:ASP185 4.7 35.6 1.0 CA A:PRO223 4.7 28.8 1.0 CB A:ASP179 4.7 26.0 1.0 CA A:ASP181 4.7 28.4 1.0 N A:ASN180 4.7 29.4 1.0 C A:GLY182 4.8 32.0 1.0 N A:ARG178 4.8 33.6 1.0 C A:PRO223 4.8 30.9 1.0 CA A:PRO184 4.8 31.5 1.0 O A:PRO184 4.9 29.5 1.0 C A:ASP181 4.9 27.2 1.0 CA A:ASP179 5.0 28.4 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.7-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 1.7-A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca801 b:26.4 occ:1.00 OD2 A:ASP179 2.3 29.9 1.0 OD2 A:ASP235 2.4 23.8 1.0 OD2 A:ASP181 2.4 25.8 1.0 O A:SER222 2.4 26.2 1.0 O A:LYS225 2.4 23.7 1.0 OE1 A:GLU188 2.4 29.5 1.0 OE2 A:GLU188 2.9 27.6 1.0 CD A:GLU188 3.0 28.8 1.0 CG A:ASP179 3.4 30.0 1.0 CG A:ASP235 3.5 26.5 1.0 C A:LYS225 3.5 25.8 1.0 CG A:ASP181 3.5 28.2 1.0 C A:SER222 3.5 25.3 1.0 OD1 A:ASP179 3.9 28.6 1.0 OG1 A:THR228 4.0 23.3 1.0 CB A:ASP235 4.0 24.4 1.0 OD1 A:ASP181 4.1 28.4 1.0 O A:TRP226 4.1 24.8 1.0 CA A:CA800 4.3 27.5 1.0 N A:LYS225 4.3 29.8 1.0 N A:TRP226 4.3 25.3 1.0 CA A:PRO223 4.3 28.8 1.0 CA A:TRP226 4.3 29.5 1.0 C A:TRP226 4.4 30.1 1.0 N A:PRO223 4.4 27.7 1.0 CA A:LYS225 4.4 27.3 1.0 C A:PRO223 4.5 30.9 1.0 N A:SER222 4.5 25.8 1.0 OD1 A:ASP235 4.5 26.5 1.0 CG A:GLU188 4.5 27.3 1.0 CA A:SER222 4.5 29.4 1.0 CB A:ASP179 4.6 26.0 1.0 CB A:ASP181 4.6 25.0 1.0 OG A:SER221 4.6 27.9 1.0 CB A:SER221 4.6 28.3 1.0 N A:GLU224 4.8 28.0 1.0 O A:PRO223 4.8 28.9 1.0 CB A:LYS225 5.0 26.6 1.0 C A:SER221 5.0 24.9 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