Tungsten in PDB 5c66: E. Coli Alkaline Phosphatase in Complex with Tungstate

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

The structure of E. Coli Alkaline Phosphatase in Complex with Tungstate, PDB code: 5c66 was solved by A.Peck, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.74 / 2.03
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	161.260, 161.260, 139.432, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 24

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

Zinc

(Zn)

6 atoms

The binding sites of Tungsten atom in the E. Coli Alkaline Phosphatase in Complex with Tungstate (pdb code 5c66). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total 2 binding sites of Tungsten where determined in the E. Coli Alkaline Phosphatase in Complex with Tungstate, PDB code: 5c66:
Jump to Tungsten binding site number: 1; 2;

Tungsten binding site 1 out of 2 in the E. Coli Alkaline Phosphatase in Complex with Tungstate


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of E. Coli Alkaline Phosphatase in Complex with Tungstate within 5.0Å range: probe atom residue distance (Å) B Occ A:W504 b:55.0 occ:0.50 W A:WO4504 0.0 55.0 0.5 O1 A:WO4504 2.0 30.1 0.5 O2 A:WO4504 2.0 25.1 0.5 O A:HOH660 2.1 24.4 0.5 OG A:SER102 2.2 35.6 1.0 O4 A:WO4504 2.2 36.0 0.5 O3 A:WO4504 2.2 34.9 0.5 O A:HOH607 2.4 24.5 0.5 ZN A:ZN502 2.9 31.3 1.0 CB A:SER102 3.2 35.2 1.0 ZN A:ZN501 3.2 32.2 1.0 O A:HOH609 3.4 30.8 1.0 CE1 A:HIS412 3.7 34.6 1.0 OD2 A:ASP327 3.7 37.4 1.0 NE2 A:HIS412 3.7 33.0 1.0 N A:SER102 3.7 31.4 1.0 NH1 A:ARG166 3.8 33.1 1.0 NH2 A:ARG166 3.8 40.5 1.0 O A:HOH601 4.0 31.9 1.0 CA A:SER102 4.1 33.5 1.0 CZ A:ARG166 4.3 41.3 1.0 OD1 A:ASP51 4.3 31.9 1.0 CG A:ASP327 4.3 32.0 1.0 OD1 A:ASP327 4.4 32.4 1.0 NE2 A:HIS370 4.4 33.5 1.0 OD2 A:ASP51 4.5 31.9 1.0 NE2 A:HIS331 4.6 28.2 1.0 OD2 A:ASP369 4.8 28.4 1.0 C A:ASP101 4.8 29.2 1.0 CG A:ASP51 4.8 33.2 1.0 ND1 A:HIS412 5.0 32.9 1.0

Tungsten binding site 2 out of 2 in the E. Coli Alkaline Phosphatase in Complex with Tungstate


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 2 of E. Coli Alkaline Phosphatase in Complex with Tungstate within 5.0Å range: probe atom residue distance (Å) B Occ B:W504 b:58.2 occ:0.50 W B:WO4504 0.0 58.2 0.5 O B:HOH611 1.8 22.1 0.5 O1 B:WO4504 2.0 31.0 0.5 O2 B:WO4504 2.0 25.3 0.5 OG B:SER102 2.1 35.5 1.0 O3 B:WO4504 2.2 27.7 0.5 O4 B:WO4504 2.2 36.2 0.5 O B:HOH603 2.3 22.5 0.5 ZN B:ZN501 2.9 31.7 1.0 CB B:SER102 3.1 34.2 1.0 ZN B:ZN502 3.2 31.1 1.0 O B:HOH601 3.5 37.8 1.0 N B:SER102 3.7 32.0 1.0 CE1 B:HIS412 3.7 35.7 1.0 NH1 B:ARG166 3.7 34.8 1.0 NH2 B:ARG166 3.7 33.1 1.0 OD2 B:ASP327 3.8 32.9 1.0 NE2 B:HIS412 3.8 35.4 1.0 CA B:SER102 4.0 33.1 1.0 O B:HOH602 4.0 32.1 1.0 CZ B:ARG166 4.2 40.4 1.0 NE2 B:HIS370 4.3 31.4 1.0 OD1 B:ASP51 4.3 29.8 1.0 CG B:ASP327 4.4 33.1 1.0 OD1 B:ASP327 4.4 32.8 1.0 OD2 B:ASP51 4.5 31.2 1.0 NE2 B:HIS331 4.7 28.4 1.0 C B:ASP101 4.8 30.8 1.0 OD2 B:ASP369 4.8 33.0 1.0 CG B:ASP51 4.8 32.2 1.0

A.Peck, F.Sunden, L.D.Andrews, V.S.Pande, D.Herschlag. Tungstate As A Transition State Analog For Catalysis By Alkaline Phosphatase. J.Mol.Biol. V. 428 2758 2016.
ISSN: ESSN 1089-8638
PubMed: 27189921
DOI: 10.1016/J.JMB.2016.05.007