Calcium in PDB 2y8h: Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss

The structure of Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss, PDB code: 2y8h was solved by H.Y.Cho, H.J.Cho, B.S.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.24 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.740, 86.764, 100.459, 90.00, 90.00, 90.00
R / Rfree (%)	20.988 / 25.585

The structure of Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Calcium atom in the Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss (pdb code 2y8h). 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 Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss, PDB code: 2y8h:

Calcium binding site 1 out of 1 in the Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the First Gaf Domain E87G Mutant of Mycobacterium Tuberculosis Doss within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1210 b:31.9 occ:1.00 O A:HOH2086 2.3 34.0 1.0 OD1 A:ASP183 2.5 16.5 1.0 O A:HOH2142 2.5 30.4 1.0 O A:HOH2138 2.6 24.8 1.0 OD2 A:ASP183 2.8 21.4 1.0 CG A:ASP183 3.0 19.7 1.0 NH2 A:ARG132 4.2 18.0 1.0 O A:HOH2141 4.2 26.3 1.0 NH1 A:ARG132 4.4 16.8 1.0 O A:HOH2137 4.4 11.2 1.0 CB A:ASP183 4.5 19.1 1.0 O A:HOH2084 4.6 28.1 1.0 O A:HOH2140 4.6 40.5 1.0 O A:HOH2057 4.7 24.9 1.0 O A:HOH2089 4.7 37.7 1.0 CZ A:ARG132 4.7 19.2 1.0 O A:HOH2090 4.8 22.3 1.0

H.Y.Cho, H.J.Cho, M.H.Kim, B.S.Kang. Blockage of the Channel to Heme By the E87 Side Chain in the Gaf Domain of Mycobacterium Tuberculosis Doss Confers the Unique Sensitivity of Doss to Oxygen. Febs Lett. V. 585 1873 2011.
ISSN: ISSN 0014-5793
PubMed: 21536032
DOI: 10.1016/J.FEBSLET.2011.04.050