Chlorine in PDB 3qzu: Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability

All present enzymatic activity of Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability:
3.1.1.3;

The structure of Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability, PDB code: 3qzu was solved by T.Pijning, W.Augustyniak, M.T.Reetz, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.16 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.163, 45.511, 77.613, 90.00, 101.10, 90.00
R / Rfree (%)	17.3 / 22.3

The binding sites of Chlorine atom in the Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability (pdb code 3qzu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability, PDB code: 3qzu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl182 b:13.5 occ:1.00 OG A:SER77 2.9 8.2 1.0 O A:HOH272 3.1 16.1 1.0 N A:ILE12 3.2 7.1 1.0 N A:MET78 3.3 6.1 1.0 CB A:SER77 3.4 6.5 1.0 CB A:MET78 3.5 6.2 1.0 CB A:ILE12 3.7 8.3 1.0 CG1 A:ILE12 3.7 8.4 1.0 CA A:GLY11 3.9 5.9 1.0 CD1 A:ILE12 4.0 9.7 1.0 CA A:ILE12 4.0 8.3 1.0 C A:GLY11 4.0 6.6 1.0 CA A:MET78 4.0 5.6 1.0 O A:HOH342 4.1 37.5 1.0 C A:SER77 4.3 6.6 1.0 CA A:SER77 4.5 6.3 1.0 O A:ILE12 4.5 8.4 1.0 O A:HOH336 4.6 22.5 1.0 C A:ILE12 4.8 8.6 1.0 CG A:MET78 4.8 5.8 1.0 NE2 A:HIS156 4.8 7.5 1.0 O A:HOH221 4.9 30.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Bacillus Subtilis Lipase A 7-Fold Mutant; the Outcome of Directed Evolution Towards Thermostability within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl182 b:19.5 occ:1.00 OG B:SER77 3.0 8.5 1.0 O B:HOH314 3.1 22.1 1.0 N B:ILE12 3.1 10.3 1.0 N B:MET78 3.3 8.0 1.0 CB B:SER77 3.4 8.4 1.0 CB B:MET78 3.5 8.4 1.0 CB B:ILE12 3.6 11.0 1.0 CG1 B:ILE12 3.6 10.8 1.0 CD1 B:ILE12 3.9 11.4 1.0 CA B:ILE12 3.9 11.0 1.0 CA B:GLY11 4.0 8.9 1.0 CA B:MET78 4.0 8.3 1.0 C B:GLY11 4.0 9.6 1.0 O3 B:GOL185 4.1 47.4 1.0 C B:SER77 4.3 8.0 1.0 O B:HOH340 4.3 22.5 1.0 CA B:SER77 4.5 8.1 1.0 O B:ILE12 4.5 12.1 1.0 C3 B:GOL185 4.7 46.4 1.0 CG B:MET78 4.7 10.8 1.0 C B:ILE12 4.7 11.4 1.0 NE2 B:HIS156 4.9 11.3 1.0 CG2 B:ILE12 5.0 10.0 1.0

W.Augustyniak, A.A.Brzezinska, T.Pijning, H.Wienk, R.Boelens, B.W.Dijkstra, M.T.Reetz. Biophysical Characterization of Mutants of Bacillus Subtilis Lipase Evolved For Thermostability: Factors Contributing to Increased Activity Retention. Protein Sci. V. 21 487 2012.
ISSN: ISSN 0961-8368
PubMed: 22267088
DOI: 10.1002/PRO.2031