Calcium in PDB 8brq: Crystal Structure of A Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231

The structure of Crystal Structure of A Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231, PDB code: 8brq 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)	52.53 / 1.63
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.252, 102.105, 140.079, 90, 90, 90
R / Rfree (%)	14.3 / 16.8

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

Calcium binding site 1 out of 2 in the Crystal Structure of A Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231


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 Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca605 b:15.8 occ:1.00 OE2 A:GLU154 2.3 19.4 1.0 O B:THR75 2.3 18.4 1.0 OD1 B:ASP76 2.4 17.0 1.0 OD1 B:ASN73 2.4 14.7 1.0 O B:HOH788 2.4 16.8 1.0 OE1 B:GLU256 2.5 16.5 1.0 OE2 B:GLU256 2.5 20.9 1.0 CD B:GLU256 2.8 22.0 1.0 HA B:ASP76 2.9 19.9 1.0 HD21 B:ASN73 3.2 20.7 1.0 CG B:ASN73 3.3 16.0 1.0 C B:THR75 3.4 17.6 1.0 CD A:GLU154 3.5 21.7 1.0 CG B:ASP76 3.5 16.7 1.0 ND2 B:ASN73 3.6 17.2 1.0 HH21 B:ARG203 3.7 21.7 1.0 CA B:ASP76 3.7 16.6 1.0 HG3 A:GLU154 3.8 27.0 1.0 N B:ASP76 3.9 15.6 1.0 CB B:ASP76 4.1 17.1 1.0 CG A:GLU154 4.2 22.5 1.0 H B:THR75 4.2 19.0 1.0 NH2 B:ARG203 4.2 18.1 1.0 H B:GLU256 4.2 18.9 1.0 HE B:ARG203 4.3 20.2 1.0 CG B:GLU256 4.3 16.9 1.0 O B:HOH935 4.4 27.2 1.0 OE1 A:GLU154 4.4 20.6 1.0 HG2 A:GLU154 4.4 27.0 1.0 O B:ASP209 4.4 17.9 1.0 OD2 B:ASP76 4.4 19.2 1.0 HD22 B:ASN73 4.5 20.7 1.0 O B:HOH1162 4.5 19.6 1.0 HB3 B:ASP76 4.5 20.6 1.0 HH22 B:ARG203 4.6 21.7 1.0 O B:HOH1031 4.6 18.1 1.0 HG3 B:GLU256 4.6 20.3 1.0 CA B:THR75 4.6 15.3 1.0 N B:THR75 4.7 15.8 1.0 H B:ILE77 4.7 19.4 1.0 HB3 B:GLU256 4.7 20.9 1.0 HB B:THR75 4.7 23.1 1.0 CB B:ASN73 4.7 15.6 1.0 HA B:ASN73 4.7 20.8 1.0 H B:ASP76 4.8 18.7 1.0 HA3 B:GLY255 4.8 18.4 1.0 NE B:ARG203 4.8 16.8 1.0 HG2 B:GLU256 4.8 20.3 1.0 CZ B:ARG203 4.8 16.4 1.0 O A:HOH327 4.9 20.2 1.0 HB2 B:ASP76 4.9 20.6 1.0 C B:ASP76 5.0 21.9 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of A Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231


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 Surface Entropy Reduction Variant of Penicillin G Acylase From Bacillaceae I. S. Sp. Fjat-27231 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca606 b:25.3 occ:0.85 OD1 B:ASP336 2.3 24.4 1.0 OD1 B:ASP344 2.3 23.1 1.0 O B:TYR342 2.3 24.7 1.0 OD1 B:ASP340 2.3 29.4 1.0 O B:HOH1067 2.4 31.8 1.0 OD1 B:ASN338 2.4 29.3 1.0 HA B:ASP336 3.1 25.1 1.0 CG B:ASP340 3.1 37.8 1.0 H B:TYR342 3.3 29.8 1.0 CG B:ASP336 3.4 26.5 1.0 H B:ASP340 3.5 32.3 1.0 CG B:ASN338 3.5 36.0 1.0 C B:TYR342 3.5 21.8 1.0 OD2 B:ASP340 3.5 38.6 1.0 CG B:ASP344 3.6 24.9 1.0 HA B:ASP344 3.6 24.4 1.0 HD21 B:ASN338 3.6 48.9 1.0 H B:ASN338 3.8 34.8 1.0 HB2 B:TYR342 3.9 28.3 1.0 CA B:ASP336 3.9 20.9 1.0 ND2 B:ASN338 4.0 40.8 1.0 N B:TYR342 4.1 24.8 1.0 CB B:ASP336 4.1 21.8 1.0 N B:ASP344 4.2 19.2 1.0 O B:HOH1181 4.2 49.1 1.0 CA B:ASP344 4.2 20.3 1.0 N B:ASP340 4.2 26.9 1.0 CA B:TYR342 4.2 21.5 1.0 HB2 B:ASP336 4.3 26.1 1.0 OD2 B:ASP336 4.3 25.4 1.0 C B:TYR343 4.3 23.1 1.0 CB B:ASP340 4.3 33.1 1.0 H B:HIS339 4.3 32.9 1.0 C B:ASP336 4.4 25.8 1.0 H B:LYS337 4.4 26.1 1.0 OD2 B:ASP344 4.4 27.4 1.0 HA B:TYR343 4.4 22.4 1.0 H B:ASP344 4.4 23.1 1.0 HB3 B:ASP340 4.5 39.8 1.0 H B:GLY341 4.5 33.3 1.0 O B:HOH1144 4.5 45.3 1.0 CB B:ASP344 4.5 23.8 1.0 N B:ASN338 4.5 29.0 1.0 N B:TYR343 4.5 19.7 1.0 CB B:TYR342 4.5 23.6 1.0 N B:LYS337 4.6 21.7 1.0 O B:TYR343 4.6 25.3 1.0 CA B:TYR343 4.6 18.7 1.0 N B:HIS339 4.7 27.4 1.0 CA B:ASP340 4.7 34.4 1.0 O B:GLU335 4.7 20.4 1.0 N B:GLY341 4.7 27.7 1.0 CB B:ASN338 4.8 34.9 1.0 HD3 B:ARG433 4.8 35.9 1.0 HD22 B:ASN338 4.8 48.9 1.0 C B:ASP340 4.9 29.1 1.0 HB3 B:ASP344 4.9 28.6 1.0 HB3 B:TYR342 4.9 28.3 1.0 HB3 B:ASP336 5.0 26.1 1.0 C B:ASN338 5.0 31.3 1.0 CA B:ASN338 5.0 35.4 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