Zinc in PDB 3cmr: E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate:
3.1.3.1;

The structure of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate, PDB code: 3cmr was solved by P.J.O'brien, J.K.Lassila, T.D.Fenn, J.G.Zalatan, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.75 / 2.05
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	160.614, 160.614, 139.923, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 21.3

The structure of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate (pdb code 3cmr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate, PDB code: 3cmr:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn450 b:28.7 occ:1.00 OG A:SER102 2.0 34.2 1.0 OD2 A:ASP369 2.0 33.9 1.0 OD1 A:ASP51 2.0 31.7 1.0 NE2 A:HIS370 2.2 33.3 1.0 CG A:ASP51 2.7 33.2 1.0 OD2 A:ASP51 2.8 32.4 1.0 CG A:ASP369 2.8 31.3 1.0 CB A:SER102 3.0 33.4 1.0 OD1 A:ASP369 3.0 32.2 1.0 CD2 A:HIS370 3.0 30.9 1.0 CE1 A:HIS370 3.2 34.8 1.0 CA A:SER102 3.6 32.8 1.0 O2 A:PO4452 3.7 43.6 1.0 OD1 A:ASP327 4.0 34.0 1.0 CG A:ASP327 4.0 35.2 1.0 N A:SER102 4.1 33.3 1.0 CE1 A:HIS412 4.1 34.6 1.0 CB A:ASP51 4.1 33.1 1.0 CG A:HIS370 4.2 33.3 1.0 CB A:ASP369 4.2 31.7 1.0 NE2 A:HIS412 4.2 34.0 1.0 ND1 A:HIS370 4.2 32.8 1.0 OD2 A:ASP327 4.2 35.2 1.0 O A:HOH506 4.2 24.2 1.0 N A:GLY52 4.2 34.5 1.0 ZN A:ZN451 4.3 28.9 1.0 CB A:ASP327 4.5 33.0 1.0 CA A:ASP51 4.5 32.7 1.0 C A:ASP51 4.6 33.6 1.0 O A:HOH501 4.6 26.6 1.0 MG A:MG453 4.6 29.7 1.0 O4 A:PO4452 4.6 36.8 1.0 P A:PO4452 4.6 45.0 1.0 C A:ASP101 4.9 33.5 1.0 O A:HOH557 4.9 28.1 1.0 CA A:GLY52 5.0 34.4 1.0 ND1 A:HIS412 5.0 34.5 1.0 C A:SER102 5.0 32.6 1.0 O1 A:PO4452 5.0 41.8 1.0

Zinc binding site 2 out of 4 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn451 b:28.9 occ:1.00 O1 A:PO4452 1.8 41.8 1.0 NE2 A:HIS331 2.0 31.2 1.0 NE2 A:HIS412 2.2 34.0 1.0 OD2 A:ASP327 2.2 35.2 1.0 OD1 A:ASP327 2.6 34.0 1.0 CG A:ASP327 2.7 35.2 1.0 CD2 A:HIS331 2.9 32.4 1.0 P A:PO4452 3.0 45.0 1.0 CE1 A:HIS331 3.0 35.8 1.0 CD2 A:HIS412 3.1 34.7 1.0 O2 A:PO4452 3.1 43.6 1.0 CE1 A:HIS412 3.2 34.6 1.0 O4 A:PO4452 3.8 36.8 1.0 O A:HOH557 4.0 28.1 1.0 OG A:SER102 4.0 34.2 1.0 CG A:HIS331 4.1 33.5 1.0 ND1 A:HIS331 4.1 33.3 1.0 O3 A:PO4452 4.2 42.9 1.0 O A:HOH625 4.2 52.9 1.0 NE2 A:HIS372 4.2 33.2 1.0 CB A:ASP327 4.2 33.0 1.0 ND1 A:HIS412 4.3 34.5 1.0 CG A:HIS412 4.3 33.4 1.0 ZN A:ZN450 4.3 28.7 1.0 CE1 A:HIS370 4.4 34.8 1.0 NE2 A:HIS370 4.4 33.3 1.0 OD1 A:ASP51 4.7 31.7 1.0 CD2 A:HIS372 4.8 32.8 1.0 O A:ASP327 4.8 32.4 1.0

Zinc binding site 3 out of 4 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn450 b:33.1 occ:1.00 OD2 B:ASP369 1.8 32.6 1.0 OD1 B:ASP51 2.1 32.9 1.0 OG B:SER102 2.1 33.8 1.0 NE2 B:HIS370 2.3 36.2 1.0 CG B:ASP51 2.7 33.8 1.0 CG B:ASP369 2.8 37.8 1.0 OD2 B:ASP51 2.8 30.0 1.0 CD2 B:HIS370 3.1 33.0 1.0 OD1 B:ASP369 3.1 36.1 1.0 CB B:SER102 3.1 31.9 1.0 CE1 B:HIS370 3.2 35.7 1.0 O2 B:PO4452 3.6 43.3 1.0 CA B:SER102 3.6 31.9 1.0 OD1 B:ASP327 3.8 33.8 1.0 CG B:ASP327 4.0 34.0 1.0 CB B:ASP51 4.1 34.1 1.0 CB B:ASP369 4.1 34.9 1.0 N B:SER102 4.2 32.4 1.0 CE1 B:HIS412 4.2 34.2 1.0 CG B:HIS370 4.2 35.1 1.0 ND1 B:HIS370 4.2 36.1 1.0 NE2 B:HIS412 4.2 35.2 1.0 O B:HOH509 4.2 26.5 1.0 N B:GLY52 4.3 33.1 1.0 ZN B:ZN451 4.3 29.6 1.0 OD2 B:ASP327 4.3 34.9 1.0 CA B:ASP51 4.5 34.0 1.0 O B:HOH503 4.5 33.0 1.0 CB B:ASP327 4.5 31.7 1.0 C B:ASP51 4.6 34.1 1.0 MG B:MG453 4.7 34.7 1.0 P B:PO4452 4.7 44.9 1.0 O4 B:PO4452 4.8 37.4 1.0 C B:ASP101 4.9 32.9 1.0 O B:HOH525 4.9 27.1 1.0 CA B:GLY52 5.0 34.4 1.0 ND1 B:HIS412 5.0 33.8 1.0 C B:SER102 5.0 31.8 1.0

Zinc binding site 4 out of 4 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn451 b:29.6 occ:1.00 O1 B:PO4452 1.9 41.7 1.0 NE2 B:HIS331 2.0 30.8 1.0 NE2 B:HIS412 2.1 35.2 1.0 OD2 B:ASP327 2.3 34.9 1.0 OD1 B:ASP327 2.7 33.8 1.0 CG B:ASP327 2.8 34.0 1.0 P B:PO4452 2.9 44.9 1.0 CE1 B:HIS331 3.0 31.9 1.0 CD2 B:HIS331 3.0 29.0 1.0 O2 B:PO4452 3.0 43.3 1.0 CE1 B:HIS412 3.1 34.2 1.0 CD2 B:HIS412 3.1 30.6 1.0 O4 B:PO4452 3.8 37.4 1.0 O B:HOH525 3.9 27.1 1.0 ND1 B:HIS331 4.1 34.9 1.0 O3 B:PO4452 4.1 44.9 1.0 CG B:HIS331 4.1 31.3 1.0 OG B:SER102 4.1 33.8 1.0 ND1 B:HIS412 4.2 33.8 1.0 CG B:HIS412 4.2 33.1 1.0 NE2 B:HIS372 4.3 33.8 1.0 CB B:ASP327 4.3 31.7 1.0 ZN B:ZN450 4.3 33.1 1.0 NE2 B:HIS370 4.4 36.2 1.0 CE1 B:HIS370 4.5 35.7 1.0 OD1 B:ASP51 4.7 32.9 1.0 CD2 B:HIS372 4.8 33.2 1.0 O B:ASP327 4.9 33.0 1.0

P.J.O'brien, J.K.Lassila, T.D.Fenn, J.G.Zalatan, D.Herschlag. Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of ARG166 Mutations in Escherichia Coli Alkaline Phosphatase Biochemistry V. 47 7663 2008.
ISSN: ISSN 0006-2960
PubMed: 18627128
DOI: 10.1021/BI800545N