Strontium in PDB 6ny9: Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse

All present enzymatic activity of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse:
3.1.1.93;

The structure of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse, PDB code: 6ny9 was solved by Y.Cao, P.A.Rice, B.C.Dickinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.46 / 1.66
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	99.388, 99.388, 149.597, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 21.9

The binding sites of Strontium atom in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse (pdb code 6ny9). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total 4 binding sites of Strontium where determined in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse, PDB code: 6ny9:
Jump to Strontium binding site number: 1; 2; 3; 4;

Strontium binding site 1 out of 4 in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse within 5.0Å range: probe atom residue distance (Å) B Occ B:Sr302 b:28.1 occ:0.61 O B:HOH410 2.3 18.3 1.0 OD1 B:ASN7 2.4 22.5 1.0 O B:HOH542 2.4 53.8 1.0 O B:ARG8 2.5 18.0 1.0 O B:HOH540 2.6 50.6 1.0 O B:HOH567 3.0 45.6 1.0 OD1 B:ASN13 3.0 16.2 1.0 CG B:ASN7 3.4 22.5 1.0 H B:ARG8 3.4 16.0 1.0 HD21 B:ASN13 3.4 17.1 1.0 HD21 B:ASN7 3.5 32.3 1.0 C B:ARG8 3.6 17.8 1.0 HA B:SER9 3.7 28.8 1.0 ND2 B:ASN7 3.8 22.3 1.0 CG B:ASN13 3.9 16.5 1.0 N B:ARG8 4.0 18.3 1.0 ND2 B:ASN13 4.0 16.9 1.0 HA B:ASN7 4.2 15.5 1.0 H B:GLU10 4.4 25.4 1.0 CA B:ARG8 4.4 17.8 1.0 N B:SER9 4.5 31.4 1.0 O B:LEU11 4.5 24.7 1.0 CA B:SER9 4.5 31.4 1.0 O B:HOH499 4.6 24.5 1.0 CB B:ASN7 4.6 22.8 1.0 HD22 B:ASN7 4.6 32.3 1.0 C B:ASN7 4.7 21.9 1.0 CA B:ASN7 4.7 22.5 1.0 HD22 B:ASN13 4.8 17.1 1.0 HB2 B:ASN7 4.9 19.1 1.0 N B:GLU10 5.0 34.9 1.0

Strontium binding site 2 out of 4 in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 2 of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse within 5.0Å range: probe atom residue distance (Å) B Occ B:Sr303 b:26.6 occ:0.70 O B:HOH451 2.6 22.9 1.0 O B:HOH518 2.8 33.9 1.0 O B:HOH429 2.9 24.0 1.0 O B:HOH507 3.3 31.7 1.0 O B:SER66 4.2 17.1 1.0 O B:GLY68 4.5 19.1 1.0 O B:GLY64 4.7 19.9 1.0 O B:HOH403 4.7 29.9 1.0 O B:HOH581 4.8 45.8 1.0 HA B:ASP67 4.9 12.4 1.0 HA2 B:GLY62 5.0 13.6 1.0 O B:GLY62 5.0 17.9 1.0

Strontium binding site 3 out of 4 in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 3 of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse within 5.0Å range: probe atom residue distance (Å) B Occ B:Sr304 b:65.8 occ:0.81 O B:HIS135 2.4 39.4 1.0 HA B:ALA136 3.3 39.7 1.0 C B:HIS135 3.6 38.1 1.0 HB3 B:HIS135 4.0 33.9 1.0 HE22 B:GLN142 4.1 41.2 1.0 CA B:ALA136 4.1 35.1 1.0 N B:ALA136 4.3 33.8 1.0 CA B:HIS135 4.6 37.0 1.0 C B:ALA136 4.7 37.1 1.0 HA B:HIS135 4.7 33.6 1.0 CB B:HIS135 4.8 35.8 1.0 NE2 B:GLN142 4.8 45.8 1.0 O B:ALA136 4.8 38.7 1.0 HE21 B:GLN142 4.8 41.2 1.0 O B:LEU137 5.0 45.4 1.0

Strontium binding site 4 out of 4 in the Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 4 of Alpha/Beta Hydrolase Domain-Containing Protein 10 From Mouse within 5.0Å range: probe atom residue distance (Å) B Occ B:Sr305 b:0.1 occ:0.50 O B:HOH401 2.3 33.8 1.0 O B:HOH419 3.3 38.3 1.0 OD2 B:ASP243 3.3 24.3 1.0 O B:HOH428 3.6 47.5 1.0 OD1 B:ASP244 4.1 29.3 1.0 CG B:ASP243 4.5 24.2 1.0 HB3 B:ASP243 4.7 20.9 1.0

Y.Cao, Q.Tian, R.S.Kathayat, S.A.Azizi, P.A.Rice, B.C.Dickinson. ABHD10 Regulates Mitochondrial Redox Homeostasis Through S-Depalmitoylation of PRDX5 To Be Published.