Calcium in PDB 7lv6: The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis

All present enzymatic activity of The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis:
3.2.1.10;

The structure of The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis, PDB code: 7lv6 was solved by C.J.Hamill, E.J.Prentice, C.D.Bahl, I.S.Truebridge, V.L.Arcus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.54 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.749, 100.999, 61.749, 90, 113.06, 90
R / Rfree (%)	12.6 / 14.5

The binding sites of Calcium atom in the The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis (pdb code 7lv6). 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 The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis, PDB code: 7lv6:

Calcium binding site 1 out of 1 in the The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Mall Mutant Enzyme S536R From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca703 b:10.4 occ:1.00 OD1 B:ASP20 2.3 11.5 1.0 O B:PHE26 2.3 10.8 1.0 OD2 B:ASP28 2.3 13.2 1.0 O B:HOH862 2.3 14.4 1.0 OD1 B:ASP24 2.3 12.1 1.0 OD1 B:ASN22 2.3 13.4 1.0 HB3 B:ASP28 3.2 14.3 1.0 CG B:ASP24 3.3 13.5 1.0 CG B:ASN22 3.3 14.9 1.0 H B:ASN22 3.3 16.2 1.0 CG B:ASP28 3.3 12.7 1.0 H B:PHE26 3.3 12.9 1.0 CG B:ASP20 3.4 10.6 1.0 H B:ASP24 3.4 14.5 1.0 C B:PHE26 3.5 10.0 1.0 HB3 B:PHE26 3.6 12.6 1.0 HD21 B:ASN22 3.6 22.9 1.0 HA B:ASP20 3.6 12.8 1.0 OD2 B:ASP24 3.7 16.2 1.0 CB B:ASP28 3.8 11.9 1.0 ND2 B:ASN22 3.8 19.1 1.0 H B:GLY23 4.0 16.7 1.0 N B:PHE26 4.0 10.7 1.0 N B:ASN22 4.1 13.5 1.0 OD2 B:ASP20 4.2 12.4 1.0 CA B:PHE26 4.2 10.1 1.0 CB B:ASP20 4.2 10.3 1.0 N B:ASP24 4.2 12.1 1.0 HB2 B:ASP20 4.2 12.4 1.0 CA B:ASP20 4.3 10.7 1.0 H B:ALA21 4.3 14.8 1.0 CB B:PHE26 4.3 10.5 1.0 HA2 B:GLY27 4.4 11.1 1.0 OD1 B:ASP28 4.4 14.6 1.0 N B:GLY23 4.4 13.9 1.0 CB B:ASN22 4.4 14.4 1.0 CB B:ASP24 4.5 13.3 1.0 C B:GLY27 4.5 9.9 1.0 O B:LYS73 4.5 14.7 1.0 HB2 B:ASP28 4.5 14.3 1.0 N B:ASP28 4.5 10.2 1.0 H B:GLY25 4.5 14.1 1.0 HD1 B:PHE26 4.5 14.2 1.0 N B:GLY27 4.5 9.4 1.0 CA B:ASN22 4.6 13.9 1.0 N B:ALA21 4.6 12.3 1.0 C B:ASP20 4.6 11.9 1.0 HD22 B:ASN22 4.6 22.9 1.0 C B:ASN22 4.7 14.7 1.0 HB3 B:ASP24 4.7 15.9 1.0 CA B:GLY27 4.7 9.3 1.0 H B:ASP28 4.7 12.2 1.0 CA B:ASP24 4.7 12.4 1.0 HB3 B:ASN22 4.8 17.3 1.0 CA B:ASP28 4.8 10.4 1.0 N B:GLY25 4.8 11.7 1.0 O B:GLY27 4.8 10.9 1.0 HB2 B:PHE26 4.9 12.6 1.0 C B:ASP24 4.9 12.6 1.0

C.J.Hamill, V.L.Arcus, E.J.Prentice, C.Bahl, I.Truebridge. Urea Binding to Guide Rational Design of Mutations That Influence Enzyme Dynamics To Be Published.