Nickel in PDB 8etf: Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound

The structure of Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound, PDB code: 8etf was solved by M.E.Walker, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.86 / 1.79
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	104.523, 147.994, 104.563, 90, 94.82, 90
R / Rfree (%)	18.7 / 22.2

The binding sites of Nickel atom in the Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound (pdb code 8etf). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound, PDB code: 8etf:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni402 b:41.2 occ:1.00 ND1 B:HIS328 1.9 41.4 1.0 ND1 E:HIS328 1.9 42.4 1.0 NE2 E:HIS330 2.1 45.0 1.0 NE2 B:HIS330 2.2 47.7 1.0 CE1 B:HIS328 2.7 43.2 1.0 CE1 E:HIS328 2.8 44.6 1.0 CE1 E:HIS330 2.9 40.7 1.0 CG B:HIS328 3.0 44.3 1.0 CG E:HIS328 3.0 42.0 1.0 CE1 B:HIS330 3.1 42.8 1.0 CD2 B:HIS330 3.2 44.5 1.0 CD2 E:HIS330 3.3 43.4 1.0 CB B:HIS328 3.4 43.3 1.0 CB E:HIS328 3.4 40.8 1.0 NE2 B:HIS328 3.9 43.6 1.0 NE2 E:HIS328 4.0 42.6 1.0 CD2 B:HIS328 4.0 40.7 1.0 CD2 E:HIS328 4.1 44.5 1.0 ND1 E:HIS330 4.1 41.2 1.0 ND1 B:HIS330 4.2 43.9 1.0 CG E:HIS330 4.3 42.9 1.0 CG B:HIS330 4.3 43.9 1.0 ND1 B:HIS326 4.5 40.2 1.0 CE1 B:HIS326 4.6 42.0 1.0 ND1 E:HIS326 4.7 46.1 1.0 CE1 E:HIS326 4.7 43.7 1.0 CA B:HIS328 5.0 45.5 1.0 CA E:HIS328 5.0 46.8 1.0 CG B:HIS326 5.0 40.4 1.0

Nickel binding site 2 out of 2 in the Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound within 5.0Å range: probe atom residue distance (Å) B Occ F:Ni402 b:42.6 occ:1.00 ND1 F:HIS328 1.9 44.9 1.0 NE2 F:HIS330 2.1 45.5 1.0 CE1 F:HIS328 2.8 50.4 1.0 CG F:HIS328 3.0 49.1 1.0 CE1 F:HIS330 3.1 44.5 1.0 CD2 F:HIS330 3.1 45.5 1.0 CB F:HIS328 3.5 49.4 1.0 NE2 F:HIS328 4.0 53.0 1.0 CD2 F:HIS328 4.1 50.7 1.0 ND1 F:HIS330 4.2 43.8 1.0 CG F:HIS330 4.2 47.9 1.0 ND1 F:HIS326 4.6 46.5 1.0 CE1 F:HIS326 4.7 48.7 1.0 CA F:HIS328 5.0 50.2 1.0

M.E.Walker, M.R.Redinbo. Structural Diversity of Bile Salt Hydrolases Reveals Rationale For Substrate Selectivity To Be Published.