Magnesium in PDB 9f2r: Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site

All present enzymatic activity of Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site:
2.7.7.48;

The structure of Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site, PDB code: 9f2r was solved by S.Cusack, P.Drncova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	125.80 / 1.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.08, 119.267, 251.555, 90, 90, 90
R / Rfree (%)	18.9 / 24.6

The binding sites of Magnesium atom in the Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site (pdb code 9f2r). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site, PDB code: 9f2r:

Magnesium binding site 1 out of 1 in the Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Influenza A/H17N10 Polymerase with Bound Promoter and 3' End of Template in Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:50.9 occ:1.00 O B:HOH999 2.5 34.5 1.0 OD2 B:ASP445 2.6 56.8 1.0 O B:ASN306 2.6 37.0 1.0 CG B:ASP445 3.6 53.8 1.0 OD1 B:ASP305 3.7 44.2 1.0 OD2 B:ASP305 3.8 52.8 1.0 C B:ASN306 3.9 34.1 1.0 CB B:ASP445 4.0 56.3 1.0 CG B:ASP305 4.1 40.8 1.0 O B:ASP445 4.6 42.8 1.0 CB B:TRP309 4.7 42.7 1.0 CA B:THR307 4.7 38.9 1.0 N B:THR307 4.7 34.2 1.0 OD1 B:ASP445 4.8 51.9 1.0 N B:LYS308 4.8 35.7 1.0 N B:ASN306 4.8 28.6 1.0 CA B:ASN306 4.9 33.6 1.0

S.Cusack, P.Drncova, T.Krischuns, N.Naffakh. High-Resolution Structure of A Replication-Initiation Like Configuration of Influenza Polymerase Active Site Visualises the Essential Role of A Conserved Dibasic Motif in the Pa Subunit To Be Published.