Calcium in PDB 3mhz: 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen

The structure of 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen, PDB code: 3mhz was solved by S.Lovell, K.P.Battaile, D.S.Wimalasena, B.E.Janowiak, M.Miyagi, J.Sun, J.Hajduch, C.Pooput, K.L.Kirk, J.G.Bann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.368, 93.975, 119.115, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 22.2

The structure of 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen also contains other interesting chemical elements:

Fluorine

(F)

7 atoms

The binding sites of Calcium atom in the 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen (pdb code 3mhz). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen, PDB code: 3mhz:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca736 b:22.9 occ:1.00 OD2 A:ASP181 2.3 22.2 1.0 OD2 A:ASP235 2.3 20.4 1.0 OD2 A:ASP179 2.3 26.2 1.0 O A:SER222 2.4 24.0 1.0 OE1 A:GLU188 2.4 26.4 1.0 O A:LYS225 2.4 21.4 1.0 OE2 A:GLU188 2.8 23.7 1.0 CD A:GLU188 3.0 24.7 1.0 CG A:ASP179 3.4 27.0 1.0 CG A:ASP235 3.4 22.0 1.0 C A:LYS225 3.5 21.3 1.0 CG A:ASP181 3.5 23.1 1.0 C A:SER222 3.6 23.7 1.0 OD1 A:ASP179 3.9 25.8 1.0 CB A:ASP235 4.0 21.0 1.0 OG1 A:THR228 4.0 20.4 1.0 OD1 A:ASP181 4.1 24.6 1.0 O A:TRP226 4.2 21.9 1.0 N A:LYS225 4.2 23.5 1.0 N A:TRP226 4.2 21.7 1.0 CA A:CA737 4.3 24.2 1.0 CA A:TRP226 4.3 21.4 1.0 C A:TRP226 4.3 21.7 1.0 CA A:PRO223 4.3 26.1 1.0 N A:PRO223 4.4 24.9 1.0 CA A:LYS225 4.4 22.1 1.0 CG A:GLU188 4.5 24.7 1.0 OD1 A:ASP235 4.5 21.9 1.0 C A:PRO223 4.5 27.1 1.0 N A:SER222 4.5 22.8 1.0 CA A:SER222 4.6 22.2 1.0 CB A:ASP179 4.6 26.2 1.0 CB A:ASP181 4.6 22.4 1.0 OG A:SER221 4.6 25.4 1.0 CB A:SER221 4.7 23.8 1.0 N A:GLU224 4.8 25.8 1.0 O A:PRO223 4.9 27.3 1.0 CB A:LYS225 4.9 23.0 1.0 CB A:SER222 5.0 22.6 1.0

Calcium binding site 2 out of 2 in the 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of 1.7A Structure of 2-Fluorohistidine Labeled Protective Antigen within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca737 b:24.2 occ:1.00 OE2 A:GLU188 2.3 23.7 1.0 O A:ILE183 2.3 23.6 1.0 OD1 A:ASP177 2.3 26.9 1.0 OD1 A:ASP181 2.4 24.6 1.0 OD1 A:ASP179 2.4 25.8 1.0 O A:HOH805 2.4 27.0 1.0 CG A:ASP181 3.3 23.1 1.0 CG A:ASP179 3.4 27.0 1.0 CD A:GLU188 3.4 24.7 1.0 C A:ILE183 3.4 25.5 1.0 CG A:ASP177 3.6 31.9 1.0 OD2 A:ASP181 3.6 22.2 1.0 OD2 A:ASP179 3.6 26.2 1.0 N A:ILE183 3.8 25.6 1.0 CA A:ILE183 4.0 25.6 1.0 CB A:ILE183 4.2 24.9 1.0 CG A:GLU188 4.2 24.7 1.0 O A:PRO223 4.2 27.3 1.0 N A:ASP181 4.2 23.9 1.0 CA A:CA736 4.3 22.9 1.0 CA A:ASP177 4.3 32.5 1.0 OE1 A:GLU188 4.3 26.4 1.0 OD2 A:ASP177 4.4 30.0 1.0 N A:GLY182 4.4 25.3 1.0 CB A:ASP177 4.5 32.6 1.0 CB A:ASP181 4.5 22.4 1.0 N A:PRO184 4.5 26.2 1.0 C A:ASP177 4.5 31.6 1.0 C A:PRO184 4.6 28.1 1.0 N A:ASP179 4.6 28.6 1.0 CA A:PRO223 4.6 26.1 1.0 N A:ASP185 4.7 28.1 1.0 CB A:ASP179 4.7 26.2 1.0 CA A:ASP181 4.7 23.1 1.0 N A:ASN180 4.7 28.8 1.0 C A:GLY182 4.8 27.2 1.0 OD1 A:ASP185 4.8 30.6 1.0 C A:PRO223 4.8 27.1 1.0 N A:ARG178 4.8 31.4 1.0 CA A:PRO184 4.8 26.8 1.0 O A:PRO184 4.9 27.4 1.0 C A:ASP181 4.9 23.7 1.0 CA A:ASP179 5.0 27.9 1.0

D.S.Wimalasena, B.E.Janowiak, S.Lovell, M.Miyagi, J.Sun, H.Zhou, J.Hajduch, C.Pooput, K.L.Kirk, K.P.Battaile, J.G.Bann. Evidence That Histidine Protonation of Receptor-Bound Anthrax Protective Antigen Is A Trigger For Pore Formation. Biochemistry V. 49 6973 2010.
ISSN: ISSN 0006-2960
PubMed: 20672855
DOI: 10.1021/BI100647Z