Zinc in PDB 3q3q: Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1

All present enzymatic activity of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1:
3.1.3.1;

The structure of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1, PDB code: 3q3q was solved by S.C.Bihani, M.V.Hosur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.78 / 1.95
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	87.370, 87.370, 168.160, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 18.6

The structure of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 (pdb code 3q3q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1, PDB code: 3q3q:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1559 b:30.3 occ:0.75 OD2 A:ASP345 2.0 24.2 1.0 OD1 A:ASP49 2.1 30.6 1.0 NE2 A:HIS346 2.1 27.1 1.0 OG1 A:THR89 2.1 36.5 1.0 O3P A:KOP1000 2.7 49.8 0.7 CG A:ASP49 2.8 27.8 1.0 CG A:ASP345 2.9 27.9 1.0 CD2 A:HIS346 3.0 24.3 1.0 OD2 A:ASP49 3.0 28.6 1.0 CB A:THR89 3.1 36.3 1.0 CE1 A:HIS346 3.1 25.7 1.0 OD1 A:ASP345 3.2 23.2 1.0 CA A:THR89 3.4 28.2 1.0 CG2 A:THR89 3.5 28.8 1.0 N A:THR89 3.9 29.9 1.0 OD1 A:ASP300 3.9 28.4 1.0 P A:KOP1000 3.9 45.1 0.7 NZ A:LYS171 4.0 31.5 1.0 CG A:ASP300 4.0 29.6 1.0 ZN A:ZN1561 4.1 31.2 0.8 O1P A:KOP1000 4.1 38.5 0.7 CG A:HIS346 4.1 24.7 1.0 ND1 A:HIS346 4.1 22.3 1.0 CB A:ASP49 4.2 21.8 1.0 CB A:ASP345 4.2 22.3 1.0 O2P A:KOP1000 4.3 46.5 0.7 CE1 A:HIS491 4.3 32.4 1.0 N A:GLN50 4.3 21.9 1.0 OD2 A:ASP300 4.3 30.5 1.0 NE2 A:HIS491 4.4 30.8 1.0 CA A:ASP49 4.5 22.9 1.0 CB A:ASP300 4.6 22.0 1.0 CE1 A:HIS93 4.6 29.8 1.0 C A:ASP49 4.7 22.6 1.0 C A:THR89 4.7 27.3 1.0 C A:GLU88 4.7 27.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1561 b:31.2 occ:0.75 O3P A:KOP1000 2.0 49.8 0.7 NE2 A:HIS304 2.0 37.0 1.0 NE2 A:HIS491 2.0 30.8 1.0 OD1 A:ASP300 2.2 28.4 1.0 OD2 A:ASP300 2.6 30.5 1.0 O4 A:KOP1000 2.7 52.5 0.7 CG A:ASP300 2.7 29.6 1.0 P A:KOP1000 2.8 45.1 0.7 CD2 A:HIS304 2.9 34.9 1.0 CE1 A:HIS491 3.0 32.4 1.0 CD2 A:HIS491 3.1 25.8 1.0 CE1 A:HIS304 3.1 35.5 1.0 C1 A:KOP1000 3.2 51.2 0.7 O1P A:KOP1000 3.7 38.5 0.7 NE2 A:GLN50 4.0 27.1 1.0 O2P A:KOP1000 4.0 46.5 0.7 CE1 A:HIS346 4.0 25.7 1.0 NE2 A:HIS346 4.1 27.1 1.0 CG A:HIS304 4.1 34.9 1.0 ZN A:ZN1559 4.1 30.3 0.8 ND1 A:HIS491 4.1 29.1 1.0 OG1 A:THR89 4.1 36.5 1.0 ND1 A:HIS304 4.1 37.2 1.0 CG A:HIS491 4.2 26.7 1.0 CB A:ASP300 4.2 22.0 1.0 NZ A:LYS171 4.3 31.5 1.0 OD1 A:ASP49 4.5 30.6 1.0 O A:ASP300 4.8 27.3 1.0 CA A:ASP300 5.0 25.6 1.0

S.C.Bihani, A.Das, K.S.Nilgiriwala, V.Prashar, M.Pirocchi, S.K.Apte, J.-L.Ferrer, M.V.Hosur. X-Ray Structure Reveals A New Class and Provides Insight Into Evolution of Alkaline Phosphatases Plos One V. 6 22767 2011.
ISSN: ESSN 1932-6203
PubMed: 21829507
DOI: 10.1371/JOURNAL.PONE.0022767