Zinc in PDB 1alj: Alkaline Phosphatase Mutant (H412N)

All present enzymatic activity of Alkaline Phosphatase Mutant (H412N):
3.1.3.1;

The structure of Alkaline Phosphatase Mutant (H412N), PDB code: 1alj was solved by L.Ma, T.T.Tibbitts, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	194.760, 167.740, 76.230, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / n/a

The structure of Alkaline Phosphatase Mutant (H412N) also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Alkaline Phosphatase Mutant (H412N) (pdb code 1alj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Alkaline Phosphatase Mutant (H412N), PDB code: 1alj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn451 b:45.9 occ:0.24 NE2 A:HIS370 2.2 20.7 1.0 OD2 A:ASP369 2.2 36.0 1.0 CE1 A:HIS370 2.7 24.5 1.0 OG A:SER102 2.7 29.1 1.0 OD2 A:ASP51 2.8 95.3 1.0 CG A:ASP369 3.0 28.3 1.0 OD2 A:ASP327 3.2 91.5 1.0 OD1 A:ASP369 3.2 27.4 1.0 CD2 A:HIS370 3.2 9.4 1.0 CG A:ASP51 3.3 80.9 1.0 OD1 A:ASP51 3.5 91.6 1.0 O4 A:PO4453 3.6 36.4 0.8 CG A:ASP327 3.7 99.4 1.0 ND1 A:HIS370 3.7 16.1 1.0 CB A:SER102 3.8 10.2 1.0 CG A:HIS370 4.0 8.3 1.0 N A:GLY52 4.1 9.8 1.0 CB A:ASP327 4.2 0.7 1.0 OD1 A:ASP327 4.3 97.8 1.0 O1 A:PO4453 4.3 31.8 0.8 CA A:SER102 4.3 8.9 1.0 CB A:ASP51 4.4 47.8 1.0 CB A:ASP369 4.4 16.9 1.0 P A:PO4453 4.5 21.6 0.8 C A:ASP51 4.5 13.8 1.0 O A:HOH454 4.5 50.1 0.7 MG A:MG452 4.5 51.6 1.0 CA A:ASP51 4.6 24.4 1.0 CA A:GLY52 4.6 2.0 1.0 N A:SER102 4.7 2.3 1.0 O3 A:PO4453 4.8 11.8 0.8

Zinc binding site 2 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn451 b:54.6 occ:0.41 OD2 B:ASP369 2.0 27.8 1.0 NE2 B:HIS370 2.3 4.2 1.0 OD2 B:ASP51 2.6 84.0 1.0 OG B:SER102 2.7 30.0 1.0 CG B:ASP369 2.8 17.5 1.0 CE1 B:HIS370 2.9 19.4 1.0 OD1 B:ASP369 3.0 10.7 1.0 CG B:ASP51 3.1 71.5 1.0 OD1 B:ASP51 3.2 81.5 1.0 CD2 B:HIS370 3.2 11.3 1.0 OD2 B:ASP327 3.4 98.2 1.0 CB B:SER102 3.6 4.5 1.0 O4 B:PO4453 3.8 43.0 0.9 CG B:ASP327 3.9 0.8 1.0 ND1 B:HIS370 4.0 2.2 1.0 N B:GLY52 4.1 17.0 1.0 CA B:SER102 4.1 11.0 1.0 CG B:HIS370 4.2 4.8 1.0 CB B:ASP369 4.2 14.6 1.0 CB B:ASP51 4.3 42.0 1.0 CB B:ASP327 4.4 0.3 1.0 OD1 B:ASP327 4.4 0.9 1.0 O1 B:PO4453 4.4 16.4 0.9 C B:ASP51 4.5 18.3 1.0 CA B:ASP51 4.5 19.5 1.0 N B:SER102 4.6 2.0 1.0 O B:HOH519 4.6 52.4 0.8 MG B:MG452 4.6 48.9 1.0 P B:PO4453 4.6 27.2 0.9 O B:HOH499 4.7 21.4 1.0 CA B:GLY52 4.7 6.9 1.0 O B:HOH548 4.8 23.7 1.0 O3 B:PO4453 4.9 22.0 0.9 N B:HIS370 4.9 2.2 1.0

L.Ma, T.T.Tibbitts, E.R.Kantrowitz. Escherichia Coli Alkaline Phosphatase: X-Ray Structural Studies of A Mutant Enzyme (His-412-->Asn) at One of the Catalytically Important Zinc Binding Sites. Protein Sci. V. 4 1498 1995.
ISSN: ISSN 0961-8368
PubMed: 8520475