Magnesium in PDB 8a2c: The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis

The structure of The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis, PDB code: 8a2c was solved by E.Costanzi, V.Applegate, A.Port, S.H.J.Smits, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.51 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.038, 110.002, 47.962, 90, 95.74, 90
R / Rfree (%)	14.6 / 17.9

The structure of The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis also contains other interesting chemical elements:

Chlorine

(Cl)

10 atoms

The binding sites of Magnesium atom in the The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis (pdb code 8a2c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis, PDB code: 8a2c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg613 b:37.9 occ:1.00 OD1 A:ASN280 2.2 38.9 1.0 OE1 A:GLN195 2.3 19.4 1.0 O A:PHE277 2.5 14.3 1.0 O A:HOH868 2.7 25.1 1.0 HD21 A:ASN280 3.1 38.2 1.0 CG A:ASN280 3.2 26.1 1.0 O A:HOH803 3.2 19.2 1.0 CD A:GLN195 3.5 18.3 1.0 ND2 A:ASN280 3.5 31.8 1.0 C A:PHE277 3.6 11.0 1.0 HA A:PHE277 3.7 13.6 1.0 HB3 A:GLN195 3.7 15.5 1.0 HG3 A:GLN195 3.9 20.1 1.0 CG A:GLN195 4.1 16.7 1.0 CA A:PHE277 4.2 11.3 1.0 O A:HOH954 4.2 34.5 1.0 H A:ASN280 4.3 16.4 1.0 HB3 A:PHE277 4.4 16.1 1.0 HD22 A:ASN280 4.4 38.2 1.0 CB A:GLN195 4.4 12.9 1.0 HA A:ILE278 4.4 15.5 1.0 HA A:ASN280 4.5 18.0 1.0 HD1 A:PHE277 4.5 18.4 1.0 CB A:ASN280 4.5 15.8 1.0 NE2 A:GLN195 4.6 36.0 1.0 HE22 A:GLN195 4.6 43.2 1.0 N A:ILE278 4.7 10.5 1.0 N A:ASN280 4.8 13.6 1.0 HA A:GLN195 4.8 15.1 1.0 O A:ILE278 4.8 13.4 1.0 CA A:ASN280 4.9 15.0 1.0 CB A:PHE277 4.9 13.4 1.0 O A:HOH992 4.9 48.4 1.0 C A:ILE278 4.9 11.3 1.0 CA A:ILE278 4.9 12.9 1.0 HB3 A:ASN280 5.0 18.9 1.0

Magnesium binding site 2 out of 2 in the The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of the S178A Mutant of PET40, A Petase Enzyme From An Unclassified Amycolatopsis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg506 b:32.0 occ:1.00 O B:HOH665 2.1 35.8 1.0 OD1 B:ASN280 2.3 28.1 1.0 OE1 B:GLN195 2.3 23.4 1.0 O B:PHE277 2.3 14.5 1.0 O B:HOH717 2.6 22.8 1.0 O B:HOH672 2.8 22.6 1.0 CG B:ASN280 3.3 22.0 1.0 CD B:GLN195 3.4 21.4 1.0 HD21 B:ASN280 3.4 33.6 1.0 C B:PHE277 3.5 14.6 1.0 HB3 B:GLN195 3.6 14.1 1.0 HA B:PHE277 3.6 13.5 1.0 HG3 B:GLN195 3.7 22.1 1.0 ND2 B:ASN280 3.8 28.0 1.0 CG B:GLN195 4.0 18.4 1.0 H B:ASN280 4.1 18.4 1.0 CA B:PHE277 4.1 11.3 1.0 CB B:GLN195 4.2 11.7 1.0 HA B:ILE278 4.3 14.6 1.0 HB3 B:PHE277 4.3 15.3 1.0 O B:HOH839 4.4 33.0 1.0 HA B:ASN280 4.4 15.4 1.0 HD1 B:PHE277 4.5 13.6 1.0 NE2 B:GLN195 4.5 31.9 1.0 O B:HOH882 4.5 50.4 1.0 N B:ILE278 4.6 11.4 1.0 N B:ASN280 4.6 15.3 1.0 CB B:ASN280 4.6 14.9 1.0 HA B:GLN195 4.6 15.0 1.0 HE22 B:GLN195 4.6 38.3 1.0 O B:ILE278 4.6 12.1 1.0 HD22 B:ASN280 4.6 33.6 1.0 C B:ILE278 4.7 11.8 1.0 CA B:ILE278 4.7 12.1 1.0 CA B:ASN280 4.8 12.8 1.0 CB B:PHE277 4.8 12.8 1.0 HG2 B:GLN195 4.9 22.1 1.0 O B:HOH847 4.9 36.1 1.0 HB2 B:GLN195 5.0 14.1 1.0 CA B:GLN195 5.0 12.5 1.0

H.Zhang, R.Dierkes, P.Perez-Garcia, V.Applegate, E.Costanzi, K.Partus, M.Gurschke, C.Schmeisser, S.H.J.Smits, J.Chow, W.R.Streit. The Metagenome-Derived Esterase PET40 Hydrolyses Polyethylene Terephthalate (Pet) and Is Well Conserved in the Gc-Rich Gram-Positives Amycolatopsis and Streptomyces To Be Published.