Nickel in PDB 8fao: 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: 8fao was solved by M.K.Grundy, 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)	47.75 / 2.14
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	103.332, 145.744, 103.791, 90, 94.47, 90
R / Rfree (%)	18.7 / 23.9

The binding sites of Nickel atom in the Bile Salt Hydrolase B From Lactobacillus Gasseri with Covalent Inhibitor Bound (pdb code 8fao). 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: 8fao:
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 A:Ni402 b:45.5 occ:1.00 ND1 A:HIS328 1.9 46.4 1.0 CE1 A:HIS330 2.5 50.7 1.0 CE1 A:HIS328 2.8 47.7 1.0 CG A:HIS328 3.1 45.2 1.0 NE2 A:HIS330 3.2 53.6 1.0 CB A:HIS328 3.5 45.9 1.0 ND1 A:HIS330 3.6 54.1 1.0 NE2 A:HIS328 4.0 47.7 1.0 CD2 A:HIS328 4.1 45.1 1.0 CD2 A:HIS330 4.4 53.2 1.0 ND1 A:HIS326 4.5 46.4 1.0 CG A:HIS330 4.7 49.3 1.0 CE1 A:HIS326 4.7 45.9 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 D:Ni402 b:50.4 occ:1.00 ND1 F:HIS328 1.9 49.5 1.0 ND1 D:HIS328 2.0 48.2 1.0 NE2 D:HIS330 2.1 57.2 1.0 NE2 F:HIS330 2.3 57.7 1.0 CE1 F:HIS328 2.8 54.0 1.0 CE1 D:HIS328 3.0 49.0 1.0 CG F:HIS328 3.1 54.1 1.0 CE1 D:HIS330 3.1 54.4 1.0 CG D:HIS328 3.1 51.9 1.0 CD2 D:HIS330 3.2 56.5 1.0 CE1 F:HIS330 3.2 49.5 1.0 CD2 F:HIS330 3.3 56.3 1.0 CB D:HIS328 3.5 50.8 1.0 CB F:HIS328 3.6 54.2 1.0 NE2 F:HIS328 3.9 50.1 1.0 CD2 F:HIS328 4.1 50.4 1.0 NE2 D:HIS328 4.1 47.7 1.0 CD2 D:HIS328 4.2 49.5 1.0 ND1 D:HIS330 4.2 55.2 1.0 ND1 D:HIS326 4.3 54.2 1.0 CG D:HIS330 4.3 58.7 1.0 ND1 F:HIS330 4.3 55.2 1.0 CE1 D:HIS326 4.4 50.0 1.0 CG F:HIS330 4.4 54.3 1.0 ND1 F:HIS326 4.6 50.5 1.0 CE1 F:HIS326 4.7 52.0 1.0 CG D:HIS326 4.8 53.3 1.0 NE2 D:HIS326 5.0 50.2 1.0

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