Calcium in PDB 4mb1: The Structure of Mall Mutant Enzyme G202P From Bacillus Subtilus

All present enzymatic activity of The Structure of Mall Mutant Enzyme G202P From Bacillus Subtilus:
3.2.1.10;

The structure of The Structure of Mall Mutant Enzyme G202P From Bacillus Subtilus, PDB code: 4mb1 was solved by J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.67 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.500, 101.070, 61.850, 90.00, 112.86, 90.00
R / Rfree (%)	17.3 / 20

The binding sites of Calcium atom in the The Structure of Mall Mutant Enzyme G202P From Bacillus Subtilus (pdb code 4mb1). 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 G202P From Bacillus Subtilus, PDB code: 4mb1:

Calcium binding site 1 out of 1 in the The Structure of Mall Mutant Enzyme G202P From Bacillus Subtilus


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 G202P From Bacillus Subtilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca602 b:4.8 occ:1.00 O A:PHE26 2.3 8.6 1.0 OD1 A:ASP20 2.3 9.6 1.0 O A:HOH822 2.3 7.3 1.0 OD2 A:ASP28 2.3 9.3 1.0 OD1 A:ASN22 2.3 10.4 1.0 OD1 A:ASP24 2.4 9.8 1.0 CG A:ASN22 3.3 10.7 1.0 CG A:ASP28 3.3 9.0 1.0 CG A:ASP24 3.3 10.1 1.0 CG A:ASP20 3.4 9.6 1.0 C A:PHE26 3.5 8.3 1.0 OD2 A:ASP24 3.7 10.0 1.0 CB A:ASP28 3.7 8.6 1.0 ND2 A:ASN22 3.8 10.7 1.0 N A:PHE26 4.0 9.0 1.0 N A:ASN22 4.1 10.6 1.0 CA A:PHE26 4.2 8.5 1.0 OD2 A:ASP20 4.2 10.0 1.0 CB A:ASP20 4.2 9.1 1.0 N A:ASP24 4.2 11.0 1.0 CA A:ASP20 4.3 9.0 1.0 CB A:PHE26 4.3 8.5 1.0 OD1 A:ASP28 4.3 9.0 1.0 CB A:ASN22 4.4 11.2 1.0 N A:GLY23 4.4 11.1 1.0 C A:GLY27 4.5 7.8 1.0 N A:ASP28 4.5 8.0 1.0 O A:LYS73 4.5 8.6 1.0 CB A:ASP24 4.5 10.8 1.0 N A:GLY27 4.5 7.9 1.0 CA A:ASN22 4.5 11.2 1.0 N A:ALA21 4.6 9.6 1.0 C A:ASP20 4.6 9.5 1.0 CA A:GLY27 4.6 7.8 1.0 C A:ASN22 4.7 11.4 1.0 CA A:ASP28 4.7 8.1 1.0 CA A:ASP24 4.7 10.9 1.0 N A:GLY25 4.8 10.2 1.0 O A:GLY27 4.8 7.6 1.0 C A:ASP24 5.0 10.5 1.0

J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus. Change in Heat Capacity For Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. Acs Chem.Biol. V. 8 2388 2013.
ISSN: ISSN 1554-8929
PubMed: 24015933
DOI: 10.1021/CB4005029