Zinc in PDB 1hqa: Alkaline Phosphatase (H412Q)

All present enzymatic activity of Alkaline Phosphatase (H412Q):
3.1.3.1;

The structure of Alkaline Phosphatase (H412Q), PDB code: 1hqa was solved by L.Ma, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.25
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	194.900, 167.000, 76.800, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / n/a

The binding sites of Zinc atom in the Alkaline Phosphatase (H412Q) (pdb code 1hqa). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Alkaline Phosphatase (H412Q), PDB code: 1hqa:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn450 b:36.0 occ:0.95 NE2 A:HIS331 2.2 26.7 1.0 OD1 A:ASP327 2.4 14.1 1.0 OD2 A:ASP327 2.4 16.4 1.0 CG A:ASP327 2.7 17.2 1.0 O A:HOH646 2.7 38.5 1.0 OE1 A:GLN412 3.1 41.4 1.0 CD2 A:HIS331 3.2 22.8 1.0 CE1 A:HIS331 3.3 20.1 1.0 O A:HOH668 3.3 45.8 1.0 O A:HOH647 3.5 38.9 1.0 OG A:SER102 4.0 22.4 1.0 NE2 A:HIS372 4.2 12.1 1.0 ZN A:ZN451 4.2 17.4 1.0 CE1 A:HIS370 4.2 9.1 1.0 CB A:ASP327 4.2 15.4 1.0 NE2 A:HIS370 4.2 13.9 1.0 CD A:GLN412 4.3 32.2 1.0 CG A:HIS331 4.4 23.9 1.0 ND1 A:HIS331 4.4 24.5 1.0 O A:HOH619 4.4 15.3 1.0 O A:HOH669 4.5 60.9 1.0 OD1 A:ASP51 4.6 18.2 1.0 CD2 A:HIS372 4.9 11.5 1.0 NE2 A:GLN412 4.9 31.9 1.0

Zinc binding site 2 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn451 b:17.4 occ:1.00 OD2 A:ASP369 1.9 12.9 1.0 NE2 A:HIS370 2.0 13.9 1.0 OD1 A:ASP51 2.0 18.2 1.0 OG A:SER102 2.2 22.4 1.0 CG A:ASP51 2.7 15.3 1.0 OD2 A:ASP51 2.8 14.2 1.0 CG A:ASP369 2.9 12.2 1.0 CD2 A:HIS370 2.9 6.7 1.0 CE1 A:HIS370 3.0 9.1 1.0 CB A:SER102 3.0 11.4 1.0 OD1 A:ASP369 3.2 8.4 1.0 CA A:SER102 3.5 12.0 1.0 O A:HOH646 3.8 38.5 1.0 OD1 A:ASP327 3.8 14.1 1.0 N A:SER102 3.9 7.8 1.0 ND1 A:HIS370 4.1 7.3 1.0 CG A:HIS370 4.1 2.6 1.0 CG A:ASP327 4.1 17.2 1.0 O A:HOH647 4.1 38.9 1.0 O A:HOH496 4.2 14.0 1.0 ZN A:ZN450 4.2 36.0 0.9 CB A:ASP51 4.2 11.3 1.0 CB A:ASP369 4.2 9.7 1.0 O A:HOH453 4.3 9.9 1.0 N A:GLY52 4.5 5.6 1.0 OD2 A:ASP327 4.5 16.4 1.0 CB A:ASP327 4.6 15.4 1.0 ZN A:ZN452 4.6 23.2 1.0 CA A:ASP51 4.7 10.7 1.0 C A:ASP51 4.8 10.0 1.0 C A:ASP101 4.8 10.2 1.0 C A:SER102 4.9 13.4 1.0

Zinc binding site 3 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn452 b:23.2 occ:1.02 OE2 A:GLU322 2.0 12.6 1.0 OD2 A:ASP51 2.1 14.2 1.0 O A:HOH455 2.2 9.5 1.0 O A:HOH454 2.2 7.1 1.0 OG1 A:THR155 2.2 9.4 1.0 O A:HOH453 2.3 9.9 1.0 CG A:ASP51 3.1 15.3 1.0 CD A:GLU322 3.1 8.8 1.0 CB A:THR155 3.2 7.3 1.0 OE1 A:GLU322 3.6 8.8 1.0 OD2 A:ASP153 3.6 17.7 1.0 CB A:ASP51 3.7 11.3 1.0 O A:HOH619 4.0 15.3 1.0 OD1 A:ASP51 4.1 18.2 1.0 N A:THR155 4.1 13.7 1.0 O A:HOH496 4.2 14.0 1.0 CG2 A:THR155 4.2 2.0 1.0 CA A:THR155 4.3 8.8 1.0 CG A:GLU322 4.4 3.1 1.0 OG A:SER102 4.4 22.4 1.0 CB A:SER102 4.4 11.4 1.0 CB A:ALA324 4.5 13.9 1.0 O A:HOH647 4.6 38.9 1.0 CG A:ASP153 4.6 20.7 1.0 ZN A:ZN451 4.6 17.4 1.0 O A:ALA324 4.7 18.8 1.0 CA A:ALA324 4.8 17.7 1.0 OD2 A:ASP369 4.9 12.9 1.0

Zinc binding site 4 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn450 b:34.3 occ:0.94 NE2 B:HIS331 2.1 29.1 1.0 OD1 B:ASP327 2.4 22.8 1.0 OD2 B:ASP327 2.5 18.5 1.0 O B:HOH600 2.7 22.2 1.0 CG B:ASP327 2.8 19.3 1.0 O B:HOH597 3.0 33.3 1.0 CD2 B:HIS331 3.1 25.4 1.0 CE1 B:HIS331 3.2 24.9 1.0 OE1 B:GLN412 3.2 44.9 1.0 O B:HOH598 3.4 29.4 1.0 O B:HOH596 4.0 24.7 1.0 OG B:SER102 4.1 23.2 1.0 CG B:HIS331 4.2 25.9 1.0 NE2 B:HIS372 4.3 17.1 1.0 ND1 B:HIS331 4.3 26.4 1.0 ZN B:ZN451 4.3 18.9 0.9 CB B:ASP327 4.3 15.0 1.0 CD B:GLN412 4.3 37.3 1.0 CE1 B:HIS370 4.4 6.2 1.0 NE2 B:HIS370 4.4 9.1 1.0 OD1 B:ASP51 4.7 18.0 1.0 O B:ASP327 4.9 14.7 1.0 NE2 B:GLN412 4.9 38.0 1.0

Zinc binding site 5 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn451 b:18.9 occ:0.92 OD2 B:ASP369 2.0 12.8 1.0 OD1 B:ASP51 2.0 18.0 1.0 NE2 B:HIS370 2.0 9.1 1.0 OG B:SER102 2.2 23.2 1.0 CG B:ASP51 2.8 20.0 1.0 CG B:ASP369 2.9 15.5 1.0 OD2 B:ASP51 3.0 23.4 1.0 CD2 B:HIS370 3.0 7.5 1.0 CE1 B:HIS370 3.0 6.2 1.0 CB B:SER102 3.0 12.9 1.0 OD1 B:ASP369 3.2 13.4 1.0 CA B:SER102 3.5 13.9 1.0 OD2 B:ASP327 3.7 18.5 1.0 N B:SER102 3.9 8.7 1.0 O B:HOH600 4.0 22.2 1.0 O B:HOH547 4.0 10.9 1.0 CG B:ASP327 4.1 19.3 1.0 ND1 B:HIS370 4.1 5.9 1.0 CG B:HIS370 4.1 4.4 1.0 CB B:ASP51 4.2 15.1 1.0 O B:HOH508 4.2 16.3 0.8 CB B:ASP369 4.3 8.7 1.0 ZN B:ZN450 4.3 34.3 0.9 N B:GLY52 4.5 9.7 1.0 O B:HOH598 4.5 29.4 1.0 CB B:ASP327 4.6 15.0 1.0 OD1 B:ASP327 4.6 22.8 1.0 CA B:ASP51 4.6 12.8 1.0 ZN B:ZN452 4.7 24.6 0.9 C B:ASP51 4.8 13.5 1.0 C B:ASP101 4.8 13.8 1.0 C B:SER102 4.9 13.3 1.0 O B:HOH596 5.0 24.7 1.0

Zinc binding site 6 out of 6 in the Alkaline Phosphatase (H412Q)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Alkaline Phosphatase (H412Q) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn452 b:24.6 occ:0.91 OE2 B:GLU322 2.0 18.1 1.0 OD2 B:ASP51 2.1 23.4 1.0 O B:HOH509 2.1 15.8 1.0 OG1 B:THR155 2.2 15.5 1.0 O B:HOH510 2.2 13.8 0.9 O B:HOH508 2.3 16.3 0.8 CG B:ASP51 3.1 20.0 1.0 CD B:GLU322 3.1 11.4 1.0 CB B:THR155 3.2 12.7 1.0 OE1 B:GLU322 3.5 15.3 1.0 OD2 B:ASP153 3.5 23.2 1.0 CB B:ASP51 3.7 15.1 1.0 OD1 B:ASP51 4.0 18.0 1.0 N B:THR155 4.1 16.6 1.0 CG2 B:THR155 4.1 6.5 1.0 O B:HOH547 4.1 10.9 1.0 O B:HOH596 4.2 24.7 1.0 CA B:THR155 4.3 15.6 1.0 CG B:GLU322 4.4 6.5 1.0 CB B:SER102 4.5 12.9 1.0 OG B:SER102 4.5 23.2 1.0 CB B:ALA324 4.5 11.0 1.0 CG B:ASP153 4.6 23.8 1.0 ZN B:ZN451 4.7 18.9 0.9 O B:ALA324 4.8 14.9 1.0 CA B:ALA324 4.8 15.2 1.0 OD2 B:ASP369 4.9 12.8 1.0

L.Ma, E.R.Kantrowitz. Kinetic and X-Ray Structural Studies of A Mutant Escherichia Coli Alkaline Phosphatase (His-412-->Gln) at One of the Zinc Binding Sites. Biochemistry V. 35 2394 1996.
ISSN: ISSN 0006-2960
PubMed: 8652582
DOI: 10.1021/BI9523421