Calcium in PDB 8brs: 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: 8brs 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)	46.04 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.322, 101.627, 139.435, 90, 90, 90
R / Rfree (%)	14.4 / 15.6

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 8brs). 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: 8brs:
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:Ca605 b:22.1 occ:1.00 OD1 B:ASP344 2.3 20.0 1.0 OD1 B:ASN338 2.3 24.8 1.0 OD1 B:ASP336 2.3 21.1 1.0 OD1 B:ASP340 2.3 22.9 1.0 O B:TYR342 2.4 20.2 1.0 O B:HOH1046 2.5 29.4 1.0 HA B:ASP336 3.1 23.5 1.0 CG B:ASP340 3.2 23.1 1.0 H B:ASP340 3.3 28.2 1.0 CG B:ASP336 3.4 20.1 1.0 H B:TYR342 3.4 23.3 1.0 CG B:ASN338 3.4 27.6 1.0 CG B:ASP344 3.5 21.3 1.0 HA B:ASP344 3.5 22.9 1.0 C B:TYR342 3.6 18.0 1.0 OD2 B:ASP340 3.6 28.1 1.0 HD21 B:ASN338 3.7 36.3 1.0 H B:ASN338 3.7 29.4 1.0 CA B:ASP336 3.9 19.6 1.0 ND2 B:ASN338 4.0 30.2 1.0 HB2 B:TYR342 4.0 25.0 1.0 CB B:ASP336 4.1 19.9 1.0 N B:TYR342 4.1 19.4 1.0 N B:ASP340 4.1 23.5 1.0 N B:ASP344 4.2 18.0 1.0 CA B:ASP344 4.2 19.1 1.0 HB2 B:ASP336 4.2 23.8 1.0 C B:TYR343 4.3 18.2 1.0 H B:LYS337 4.3 26.4 1.0 C B:ASP336 4.3 18.9 1.0 OD2 B:ASP336 4.3 21.6 1.0 CA B:TYR342 4.3 19.6 1.0 OD2 B:ASP344 4.3 22.6 1.0 CB B:ASP340 4.4 26.1 1.0 H B:HIS339 4.4 29.2 1.0 HA B:TYR343 4.4 21.0 1.0 O B:HOH1161 4.4 45.9 1.0 CB B:ASP344 4.4 20.8 1.0 N B:ASN338 4.5 24.5 1.0 H B:ASP344 4.5 21.6 1.0 N B:LYS337 4.5 22.0 1.0 H B:GLY341 4.5 26.8 1.0 HB3 B:ASP340 4.5 31.4 1.0 N B:TYR343 4.6 17.7 1.0 O B:TYR343 4.6 20.2 1.0 CB B:TYR342 4.6 20.8 1.0 CA B:ASP340 4.6 22.5 1.0 N B:HIS339 4.6 24.3 1.0 O B:HOH1110 4.6 43.3 1.0 CA B:TYR343 4.7 17.5 1.0 CB B:ASN338 4.7 25.6 1.0 O B:GLU335 4.7 18.2 1.0 N B:GLY341 4.8 22.3 1.0 HD22 B:ASN338 4.8 36.3 1.0 HD3 B:ARG433 4.8 28.7 0.5 HB3 B:ASP344 4.9 24.9 1.0 CA B:ASN338 4.9 24.5 1.0 C B:ASN338 4.9 26.3 1.0 C B:ASP340 4.9 21.7 1.0 HB3 B:TYR342 4.9 25.0 1.0 O B:ASP336 5.0 22.5 1.0 HB3 B:ASP336 5.0 23.8 1.0 HB3 B:ASN338 5.0 30.7 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:Ca606 b:13.7 occ:1.00 OE2 A:GLU154 2.3 17.3 1.0 O B:THR75 2.3 14.5 1.0 OD1 B:ASP76 2.4 15.0 1.0 OD1 B:ASN73 2.4 14.6 1.0 O B:HOH840 2.4 14.7 1.0 OE2 B:GLU256 2.5 16.3 1.0 OE1 B:GLU256 2.5 14.8 1.0 CD B:GLU256 2.8 14.5 1.0 HA B:ASP76 2.9 17.0 1.0 HD21 B:ASN73 3.2 18.2 1.0 CG B:ASN73 3.3 13.3 1.0 C B:THR75 3.4 14.7 1.0 CD A:GLU154 3.5 15.8 1.0 CG B:ASP76 3.5 14.4 1.0 ND2 B:ASN73 3.6 15.2 1.0 CA B:ASP76 3.7 14.2 1.0 HH21 B:ARG203 3.8 18.4 1.0 HG3 A:GLU154 3.8 17.8 1.0 N B:ASP76 4.0 14.7 1.0 H B:THR75 4.1 18.4 1.0 CB B:ASP76 4.2 15.2 1.0 CG A:GLU154 4.2 14.8 1.0 NH2 B:ARG203 4.3 15.3 1.0 H B:GLU256 4.3 16.6 1.0 HE B:ARG203 4.3 19.4 1.0 CG B:GLU256 4.3 15.0 1.0 HG2 A:GLU154 4.4 17.8 1.0 OE1 A:GLU154 4.4 16.4 1.0 O A:HOH400 4.4 20.6 1.0 OD2 B:ASP76 4.4 16.3 1.0 HD22 B:ASN73 4.5 18.2 1.0 O B:ASP209 4.5 15.8 1.0 O B:HOH1136 4.5 17.0 1.0 HB3 B:ASP76 4.6 18.2 1.0 HH22 B:ARG203 4.6 18.4 1.0 HB B:THR75 4.6 20.0 1.0 CA B:THR75 4.6 14.8 1.0 O B:HOH1035 4.6 16.3 1.0 HG3 B:GLU256 4.6 18.0 1.0 N B:THR75 4.6 15.3 1.0 HB3 B:GLU256 4.7 16.7 1.0 H B:ILE77 4.7 17.8 1.0 CB B:ASN73 4.7 15.6 1.0 HA B:ASN73 4.7 17.0 1.0 HA3 B:GLY255 4.7 16.9 1.0 H B:ASP76 4.8 17.6 1.0 NE B:ARG203 4.8 16.1 1.0 HG2 B:GLU256 4.8 18.0 1.0 CZ B:ARG203 4.8 15.8 1.0 O B:HOH762 4.9 17.5 1.0 HB2 B:ASP76 4.9 18.2 1.0 HB2 B:ASP209 5.0 19.6 1.0 C B:ASP76 5.0 16.0 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