Calcium in PDB 4lxf: Crystal Structure of M. Tuberculosis Tres

All present enzymatic activity of Crystal Structure of M. Tuberculosis Tres:
5.4.99.16;

The structure of Crystal Structure of M. Tuberculosis Tres, PDB code: 4lxf was solved by R.Roy, G.S.Besra, K.Futterer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.20 / 2.60
Space group	P 32 1 2
Cell size a, b, c (Å), α, β, γ (°)	161.640, 161.640, 139.110, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 24

The binding sites of Calcium atom in the Crystal Structure of M. Tuberculosis Tres (pdb code 4lxf). 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 M. Tuberculosis Tres, PDB code: 4lxf:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of M. Tuberculosis Tres


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 M. Tuberculosis Tres within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:51.7 occ:1.00 ND2 A:ASN140 2.4 58.8 1.0 O A:HOH812 2.4 46.8 1.0 OD2 A:ASP208 2.4 63.5 1.0 OE2 A:GLU245 2.5 64.5 1.0 O A:TYR242 2.5 59.1 1.0 O A:LEU243 2.6 61.0 1.0 C A:LEU243 3.3 59.9 1.0 CD A:GLU245 3.4 64.9 1.0 CG A:ASP208 3.4 64.3 1.0 C A:TYR242 3.5 57.9 1.0 OE1 A:GLU245 3.5 66.4 1.0 CG A:ASN140 3.5 58.3 1.0 CA A:LEU243 3.6 58.8 1.0 CB A:ASP208 3.7 65.1 1.0 OD1 A:ASN140 3.9 58.3 1.0 O A:LEU209 4.0 65.8 1.0 N A:LEU243 4.0 57.7 1.0 O A:ASN140 4.2 62.5 1.0 N A:PHE244 4.4 60.3 1.0 OD1 A:ASP208 4.6 64.9 1.0 CD1 A:TRP199 4.6 65.2 1.0 NE1 A:TRP199 4.7 63.9 1.0 CA A:TYR242 4.7 57.2 1.0 CB A:TYR242 4.8 58.0 1.0 CG A:GLU245 4.8 64.1 1.0 CB A:ASN140 4.8 57.7 1.0 CA A:ASP208 4.8 64.9 1.0 CA A:PHE244 5.0 61.3 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of M. Tuberculosis Tres


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 M. Tuberculosis Tres within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca701 b:82.8 occ:1.00 ND2 B:ASN140 2.4 78.7 1.0 O B:LEU243 2.6 82.4 1.0 O B:TYR242 2.7 78.3 1.0 OD2 B:ASP208 2.7 78.6 1.0 OE1 B:GLU245 3.0 86.0 1.0 OE2 B:GLU245 3.1 87.7 1.0 C B:LEU243 3.4 81.5 1.0 CD B:GLU245 3.4 87.7 1.0 CG B:ASP208 3.5 78.6 1.0 CG B:ASN140 3.7 76.0 1.0 CB B:ASP208 3.7 79.8 1.0 C B:TYR242 3.7 76.4 1.0 O B:LEU209 3.8 83.2 1.0 CA B:LEU243 3.8 78.7 1.0 N B:LEU243 4.2 76.5 1.0 O B:ASN140 4.2 77.6 1.0 OD1 B:ASN140 4.2 75.6 1.0 N B:PHE244 4.4 83.1 1.0 CD1 B:TRP199 4.4 78.8 1.0 OD1 B:ASP208 4.7 78.8 1.0 NE1 B:TRP199 4.7 78.5 1.0 CA B:ASP208 4.8 79.1 1.0 CB B:ASN140 4.8 74.3 1.0 N B:LEU209 4.9 80.1 1.0 CA B:PHE244 4.9 84.7 1.0 C B:LEU209 4.9 84.0 1.0 CG B:GLU245 5.0 89.4 1.0 CA B:TYR242 5.0 74.8 1.0

R.Roy, V.Usha, A.Kermani, D.J.Scott, E.I.Hyde, G.S.Besra, L.J.Alderwick, K.Futterer. Synthesis of Alpha-Glucan in Mycobacteria Involves A Hetero-Octameric Complex of Trehalose Synthase Tres and Maltokinase PEP2. Acs Chem.Biol. V. 8 2245 2013.
ISSN: ISSN 1554-8929
PubMed: 23901909
DOI: 10.1021/CB400508K