Tungsten in PDB 1e3p: Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme

All present enzymatic activity of Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme:
2.7.7.8;

The structure of Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme, PDB code: 1e3p was solved by M.F.Symmons, G.H.Jones, B.F.Luisi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.84 / 2.50
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	130.830, 130.830, 328.732, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 24.7

The binding sites of Tungsten atom in the Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme (pdb code 1e3p). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme, PDB code: 1e3p:

Tungsten binding site 1 out of 1 in the Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Tungstate Derivative of Streptomyces Antibioticus Pnpase/Gpsi Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:W911 b:74.1 occ:0.37 W A:WO4911 0.0 74.1 0.4 O3 A:WO4911 1.7 73.4 0.4 O1 A:WO4911 1.7 73.9 0.4 O4 A:WO4911 1.7 73.2 0.4 O2 A:WO4911 1.7 72.8 0.4 N A:THR462 3.5 58.5 1.0 CA A:SER461 3.6 63.9 1.0 CE1 A:HIS427 3.7 47.6 1.0 OG1 A:THR462 3.7 59.2 1.0 NE2 A:HIS427 3.7 48.4 1.0 C A:SER461 4.0 62.0 1.0 N A:SER463 4.1 49.3 1.0 ND1 A:HIS427 4.2 49.1 1.0 CD2 A:HIS427 4.3 47.9 1.0 OG A:SER461 4.3 59.8 1.0 OG A:SER463 4.3 52.6 1.0 N A:SER461 4.4 65.2 1.0 CE A:LYS522 4.4 38.8 1.0 CB A:SER461 4.4 64.1 1.0 CA A:THR462 4.5 55.9 1.0 CG A:HIS427 4.5 44.1 1.0 O A:HOH2305 4.5 44.3 1.0 CB A:THR462 4.7 56.1 1.0 O A:HOH2248 4.8 35.8 1.0 CB A:SER463 4.8 48.6 1.0 C A:THR462 4.8 51.9 1.0

M.F.Symmons, G.H.Jones, B.F.Luisi. A Duplicated Fold Is the Structural Basis For Polynucleotide Phosphorylase Catalytic Activity, Processivity, and Regulation Structure V. 8 1215 2000.
ISSN: ISSN 0969-2126
PubMed: 11080643
DOI: 10.1016/S0969-2126(00)00521-9