Zinc in PDB 5xwk: Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate

All present enzymatic activity of Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate:
3.1.3.1;

The structure of Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate, PDB code: 5xwk 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)	77.00 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.990, 86.990, 165.484, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.4

The structure of Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate (pdb code 5xwk). 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 Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate, PDB code: 5xwk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate


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 Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:17.2 occ:0.75 OG1 A:THR89 1.9 20.6 1.0 OD2 A:ASP345 2.0 10.2 1.0 OD1 A:ASP49 2.0 13.0 1.0 NE2 A:HIS346 2.1 13.9 1.0 O3 A:PO4605 2.4 26.8 0.8 CG A:ASP49 2.8 13.3 1.0 CG A:ASP345 2.9 11.4 1.0 CB A:THR89 3.0 20.7 1.0 CD2 A:HIS346 3.0 12.3 1.0 OD2 A:ASP49 3.0 13.3 1.0 CE1 A:HIS346 3.1 12.2 1.0 OD1 A:ASP345 3.2 10.4 1.0 CA A:THR89 3.3 11.1 1.0 CG2 A:THR89 3.5 18.6 1.0 P A:PO4605 3.7 26.8 0.8 OD1 A:ASP300 3.8 13.4 1.0 N A:THR89 3.9 11.5 1.0 CG A:ASP300 4.0 14.1 1.0 ZN A:ZN603 4.1 13.9 0.8 O2 A:PO4605 4.1 27.0 0.8 NZ A:LYS171 4.1 17.2 1.0 CG A:HIS346 4.1 12.2 1.0 O4 A:PO4605 4.1 24.6 0.8 ND1 A:HIS346 4.2 9.8 1.0 CB A:ASP49 4.2 12.6 1.0 CE1 A:HIS491 4.3 14.5 1.0 CB A:ASP345 4.3 9.9 1.0 N A:GLN50 4.3 8.9 1.0 OD2 A:ASP300 4.3 14.0 1.0 NE2 A:HIS491 4.5 15.0 1.0 CA A:ASP49 4.5 11.3 1.0 CB A:ASP300 4.6 11.9 1.0 CE1 A:HIS93 4.7 15.3 1.0 C A:THR89 4.7 11.8 1.0 C A:ASP49 4.7 10.1 1.0 C A:GLU88 4.7 11.8 1.0 O1 A:PO4605 4.8 24.5 0.8

Zinc binding site 2 out of 2 in the Crystal Structure of Spap, An Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate


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 Alkaline Phosphatase From Sphingomonas in Complex with Inorganic Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn603 b:13.9 occ:0.75 NE2 A:HIS304 2.0 16.6 1.0 NE2 A:HIS491 2.0 15.0 1.0 OD1 A:ASP300 2.1 13.4 1.0 O3 A:PO4605 2.1 26.8 0.8 O1 A:PO4605 2.3 24.5 0.8 OD2 A:ASP300 2.6 14.0 1.0 CG A:ASP300 2.7 14.1 1.0 P A:PO4605 2.8 26.8 0.8 CE1 A:HIS491 2.9 14.5 1.0 CD2 A:HIS304 3.0 16.7 1.0 CE1 A:HIS304 3.0 19.0 1.0 CD2 A:HIS491 3.1 15.7 1.0 O4 A:PO4605 3.7 24.6 0.8 O2 A:PO4605 3.9 27.0 0.8 CE1 A:HIS346 4.0 12.2 1.0 NE2 A:HIS346 4.0 13.9 1.0 OG1 A:THR89 4.0 20.6 1.0 NE2 A:GLN50 4.1 10.8 1.0 ZN A:ZN602 4.1 17.2 0.8 ND1 A:HIS304 4.1 19.7 1.0 ND1 A:HIS491 4.1 13.4 1.0 CG A:HIS304 4.1 16.5 1.0 CB A:ASP300 4.2 11.9 1.0 CG A:HIS491 4.2 14.2 1.0 NZ A:LYS171 4.3 17.2 1.0 OD1 A:ASP49 4.4 13.0 1.0 O A:ASP300 4.9 12.0 1.0 CA A:ASP300 5.0 11.9 1.0

S.C.Bihani, S.C.Bihani, M.V.Hosur. N/A N/A.