Calcium in PDB 8brt: Crystal Structure of A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact

The structure of Crystal Structure of A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact, PDB code: 8brt was solved by J.Wichmann, J.Mayer, H.Mattes, P.Lukat, W.Blankenfeldt, R.Biedendieck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.05 / 1.31
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.314, 101.221, 139.493, 90, 90, 90
R / Rfree (%)	14.9 / 16.1

The binding sites of Calcium atom in the Crystal Structure of A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact (pdb code 8brt). 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 A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact, PDB code: 8brt:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact


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 A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca604 b:25.9 occ:1.00 OD1 B:ASP344 2.3 23.9 1.0 OD1 B:ASP336 2.3 23.7 1.0 OD1 B:ASP340 2.3 24.3 1.0 OD1 B:ASN338 2.3 26.4 1.0 O B:TYR342 2.3 23.5 1.0 O B:HOH1025 2.4 30.1 1.0 HA B:ASP336 3.1 26.5 1.0 CG B:ASP340 3.2 26.8 1.0 H B:ASP340 3.4 31.6 1.0 H B:TYR342 3.4 25.3 1.0 CG B:ASP336 3.4 24.7 1.0 CG B:ASN338 3.5 31.5 1.0 C B:TYR342 3.5 20.7 1.0 HA B:ASP344 3.5 26.0 1.0 CG B:ASP344 3.5 24.7 1.0 OD2 B:ASP340 3.6 30.1 1.0 HD21 B:ASN338 3.7 43.1 1.0 H B:ASN338 3.7 33.7 1.0 CA B:ASP336 3.9 22.1 1.0 ND2 B:ASN338 4.0 35.9 1.0 HB2 B:TYR342 4.0 29.6 1.0 N B:TYR342 4.1 21.1 1.0 CB B:ASP336 4.1 22.8 1.0 N B:ASP344 4.1 22.0 1.0 CA B:ASP344 4.2 21.6 1.0 N B:ASP340 4.2 26.4 1.0 HB2 B:ASP336 4.2 27.4 1.0 C B:TYR343 4.2 22.0 1.0 CA B:TYR342 4.3 23.5 1.0 H B:LYS337 4.3 30.7 1.0 OD2 B:ASP336 4.3 25.6 1.0 C B:ASP336 4.3 20.8 1.0 OD2 B:ASP344 4.4 25.2 1.0 CB B:ASP340 4.4 29.8 1.0 HA B:TYR343 4.4 23.7 1.0 H B:ASP344 4.4 26.4 1.0 CB B:ASP344 4.4 23.8 1.0 H B:HIS339 4.5 31.8 1.0 N B:ASN338 4.5 28.1 1.0 O B:TYR343 4.5 24.3 1.0 N B:LYS337 4.5 25.6 1.0 N B:TYR343 4.5 20.1 1.0 H B:GLY341 4.6 29.1 1.0 CB B:TYR342 4.6 24.7 1.0 HB3 B:ASP340 4.6 35.7 1.0 CA B:TYR343 4.7 19.7 1.0 N B:HIS339 4.7 26.5 1.0 CA B:ASP340 4.7 29.1 1.0 CB B:ASN338 4.7 28.1 1.0 O B:GLU335 4.7 20.4 1.0 N B:GLY341 4.8 24.3 1.0 HD22 B:ASN338 4.8 43.1 1.0 HB3 B:ASP344 4.9 28.6 1.0 C B:ASN338 4.9 31.1 1.0 HB3 B:TYR342 4.9 29.6 1.0 CA B:ASN338 4.9 25.3 1.0 C B:ASP340 4.9 25.2 1.0 HB3 B:ASP336 5.0 27.4 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact


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 A Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 with Reduced Surface Entropy and Additionally Engineered Crystal Contact within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca605 b:14.5 occ:1.00 OE2 A:GLU154 2.3 18.2 1.0 O B:THR75 2.3 15.7 1.0 OD1 B:ASN73 2.3 15.1 1.0 OD1 B:ASP76 2.4 16.1 1.0 O B:HOH780 2.4 16.5 1.0 OE2 B:GLU256 2.4 18.4 1.0 OE1 B:GLU256 2.5 16.7 1.0 CD B:GLU256 2.8 17.3 1.0 HA B:ASP76 2.9 18.7 1.0 HD21 B:ASN73 3.1 19.5 1.0 CG B:ASN73 3.3 15.2 1.0 C B:THR75 3.4 16.6 1.0 CD A:GLU154 3.5 16.6 1.0 CG B:ASP76 3.5 16.7 1.0 ND2 B:ASN73 3.6 16.3 1.0 CA B:ASP76 3.7 15.6 1.0 HH21 B:ARG203 3.7 20.8 1.0 HG3 A:GLU154 3.8 20.6 1.0 N B:ASP76 4.0 16.0 1.0 H B:THR75 4.1 19.9 1.0 CB B:ASP76 4.1 17.5 1.0 CG A:GLU154 4.2 17.1 1.0 NH2 B:ARG203 4.2 17.3 1.0 HE B:ARG203 4.3 21.9 1.0 H B:GLU256 4.3 17.5 1.0 CG B:GLU256 4.3 15.5 1.0 HG2 A:GLU154 4.4 20.6 1.0 O A:HOH405 4.4 21.7 1.0 OE1 A:GLU154 4.4 19.2 1.0 HD22 B:ASN73 4.4 19.5 1.0 O B:ASP209 4.5 17.4 1.0 OD2 B:ASP76 4.5 17.9 1.0 O B:HOH1140 4.5 19.4 1.0 HB3 B:ASP76 4.5 21.0 1.0 HB B:THR75 4.6 21.9 1.0 HH22 B:ARG203 4.6 20.8 1.0 HG3 B:GLU256 4.6 18.6 1.0 CA B:THR75 4.6 15.4 1.0 N B:THR75 4.6 16.6 1.0 O B:HOH1062 4.6 17.6 1.0 HB3 B:GLU256 4.7 19.5 1.0 H B:ILE77 4.7 19.1 1.0 HA B:ASN73 4.7 18.6 1.0 CB B:ASN73 4.7 16.3 1.0 HA3 B:GLY255 4.7 19.0 1.0 H B:ASP76 4.8 19.2 1.0 NE B:ARG203 4.8 18.3 1.0 HG2 B:GLU256 4.8 18.6 1.0 CZ B:ARG203 4.8 16.8 1.0 O B:HOH750 4.9 19.9 1.0 HB2 B:ASP76 4.9 21.0 1.0 C B:ASP76 5.0 17.4 1.0 HB2 B:ASP209 5.0 23.1 1.0

J.Wichmann, J.Mayer, M.Hintmann, P.Lukat, W.Blankenfeldt, R.Biedendieck. Multistep Engineering of A Penicillin G Acylase For Systematic Improvement of Crystallization Efficiency Cryst.Growth Des. 2023.
ISSN: ESSN 1528-7505
DOI: 10.1021/ACS.CGD.2C01408