Potassium in PDB 6nzg: Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine

All present enzymatic activity of Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine:
3.2.1.23; 3.2.1.31;

The structure of Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine, PDB code: 6nzg was solved by S.J.Pellock, P.B.Jariwala, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.46 / 2.43
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.536, 142.407, 180.664, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 22.1

The structure of Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Potassium atom in the Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine (pdb code 6nzg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine, PDB code: 6nzg:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine within 5.0Å range: probe atom residue distance (Å) B Occ A:K903 b:39.9 occ:1.00 O A:THR776 2.6 40.2 1.0 OD1 A:ASN724 2.6 39.5 1.0 O A:LEU773 2.6 35.3 1.0 O A:ASN878 2.7 37.6 1.0 O A:VAL725 2.8 42.5 1.0 OG1 A:THR776 2.8 38.1 1.0 C A:THR776 3.4 44.2 1.0 C A:ASN878 3.7 36.6 1.0 N A:VAL725 3.7 40.6 1.0 C A:VAL725 3.8 37.4 1.0 C A:LEU773 3.8 33.3 1.0 CG A:ASN724 3.8 37.0 1.0 C A:ASN724 3.9 41.8 1.0 CB A:THR776 3.9 37.2 1.0 CA A:THR776 4.0 40.2 1.0 CA A:ASN878 4.1 33.8 1.0 N A:THR776 4.2 34.6 1.0 O A:ASN724 4.2 38.5 1.0 CB A:ASN878 4.2 32.7 1.0 CA A:VAL725 4.3 41.9 1.0 N A:LEU777 4.3 43.0 1.0 CA A:ASN724 4.3 37.0 1.0 CA A:LEU773 4.4 30.9 1.0 CD1 A:LEU773 4.6 34.5 1.0 CA A:LEU777 4.6 43.7 1.0 ND2 A:ASN724 4.7 33.5 1.0 CB A:ASN724 4.7 39.5 1.0 CB A:VAL725 4.8 33.9 1.0 CB A:SER727 4.8 41.5 1.0 O A:PRO772 4.8 39.4 1.0 N A:PHE774 4.8 38.5 1.0 N A:GLY726 4.9 31.2 1.0 N A:GLY879 4.9 33.0 1.0 CG A:LEU773 5.0 37.8 1.0 O A:HOH1229 5.0 40.6 1.0

Potassium binding site 2 out of 2 in the Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Bacteroides Uniformis Beta-Glucuronidase 2 Covalently Bound to Cyclophellitol-6-Carboxylate Aziridine within 5.0Å range: probe atom residue distance (Å) B Occ B:K905 b:34.7 occ:1.00 O B:THR776 2.5 40.8 1.0 O B:LEU773 2.6 31.5 1.0 O B:ASN878 2.6 31.0 1.0 O B:VAL725 2.6 35.6 1.0 OD1 B:ASN724 2.7 32.7 1.0 OG1 B:THR776 2.7 39.5 1.0 C B:THR776 3.3 38.8 1.0 C B:VAL725 3.7 32.4 1.0 C B:ASN878 3.7 34.1 1.0 C B:LEU773 3.8 32.7 1.0 CB B:THR776 3.8 38.9 1.0 N B:VAL725 3.8 33.8 1.0 CG B:ASN724 3.8 31.9 1.0 C B:ASN724 3.9 31.5 1.0 CA B:THR776 3.9 34.6 1.0 N B:THR776 4.1 37.1 1.0 CA B:ASN878 4.2 33.3 1.0 N B:LEU777 4.2 36.3 1.0 O B:ASN724 4.3 33.9 1.0 CA B:VAL725 4.3 36.3 1.0 CA B:ASN724 4.3 31.2 1.0 CA B:LEU773 4.4 32.4 1.0 CB B:ASN878 4.5 32.1 1.0 CA B:LEU777 4.5 37.3 1.0 CD1 B:LEU773 4.5 32.1 1.0 CB B:ASN724 4.7 31.2 1.0 O B:HOH1135 4.7 33.7 1.0 CB B:SER727 4.7 36.6 1.0 ND2 B:ASN724 4.7 33.9 1.0 N B:GLY726 4.8 36.4 1.0 N B:PHE774 4.8 31.9 1.0 O B:PRO772 4.9 36.8 1.0 N B:GLY879 4.9 32.6 1.0 CB B:VAL725 4.9 35.9 1.0 N B:SER727 5.0 38.2 1.0

P.B.Jariwala, S.J.Pellock, D.Goldfarb, E.W.Cloer, M.Artola, J.B.Simpson, A.P.Bhatt, W.G.Walton, L.R.Roberts, M.B.Major, G.J.Davies, H.S.Overkleeft, M.R.Redinbo. Discovering the Microbial Enzymes Driving Drug Toxicity with Activity-Based Protein Profiling. Acs Chem.Biol. 2019.
ISSN: ESSN 1554-8937
PubMed: 31774274
DOI: 10.1021/ACSCHEMBIO.9B00788