Manganese in PDB 1hhs: Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6

All present enzymatic activity of Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6:
2.7.7.48;

The structure of Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6, PDB code: 1hhs was solved by J.M.Grimes, S.J.Butcher, E.V.Makeyev, D.H.Bamford, D.I.Stuart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.0 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	105.408, 93.364, 141.199, 90.00, 101.25, 90.00
R / Rfree (%)	22.12 / 24.87

The binding sites of Manganese atom in the Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6 (pdb code 1hhs). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6, PDB code: 1hhs:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn665 b:32.7 occ:1.00 OE1 A:GLU491 2.0 28.7 1.0 OD1 A:ASP454 2.1 28.1 1.0 O A:ALA495 2.2 34.8 1.0 O A:HOH2889 2.2 34.2 1.0 O A:HOH2888 2.3 31.4 1.0 O A:HOH2890 2.3 33.4 1.0 CD A:GLU491 3.0 33.2 1.0 CG A:ASP454 3.1 38.3 1.0 C A:ALA495 3.3 35.1 1.0 OE2 A:GLU491 3.4 33.4 1.0 OD2 A:ASP454 3.5 32.0 1.0 N A:ALA495 3.9 29.6 1.0 O A:THR323 3.9 34.1 1.0 CA A:ALA495 4.1 37.5 1.0 N A:PHE496 4.2 31.0 1.0 CG A:GLU491 4.3 31.2 1.0 CA A:PHE496 4.3 29.7 1.0 CB A:ASP454 4.4 27.3 1.0 O A:HOH2245 4.4 54.9 1.0 CB A:GLU491 4.5 30.2 1.0 O A:ALA455 4.5 31.7 1.0 N A:ALA455 4.6 33.8 1.0 CB A:ALA495 4.6 36.6 1.0 O A:HOH2689 4.6 45.1 1.0 CA A:ASP454 4.7 32.8 1.0

Manganese binding site 2 out of 3 in the Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn665 b:32.7 occ:1.00 OE1 B:GLU491 2.0 28.7 1.0 OD1 B:ASP454 2.1 28.1 1.0 O B:ALA495 2.2 34.8 1.0 O B:HOH2936 2.2 34.2 1.0 O B:HOH2938 2.3 31.4 1.0 O B:HOH2937 2.3 33.4 1.0 CD B:GLU491 3.0 33.2 1.0 CG B:ASP454 3.1 38.3 1.0 C B:ALA495 3.3 35.1 1.0 OE2 B:GLU491 3.4 33.4 1.0 OD2 B:ASP454 3.5 32.0 1.0 N B:ALA495 3.9 29.6 1.0 O B:THR323 3.9 34.1 1.0 CA B:ALA495 4.1 37.5 1.0 N B:PHE496 4.2 31.0 1.0 CG B:GLU491 4.3 31.2 1.0 CA B:PHE496 4.3 29.7 1.0 CB B:ASP454 4.4 27.3 1.0 O B:HOH2264 4.4 54.9 1.0 CB B:GLU491 4.5 30.2 1.0 O B:ALA455 4.5 31.7 1.0 N B:ALA455 4.6 33.8 1.0 CB B:ALA495 4.6 36.6 1.0 O B:HOH2727 4.6 45.1 1.0 CA B:ASP454 4.7 32.8 1.0

Manganese binding site 3 out of 3 in the Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Rna Dependent Rna Polymerase From Dsrna Bacteriophage PHI6 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn665 b:32.7 occ:1.00 OE1 C:GLU491 2.0 28.7 1.0 OD1 C:ASP454 2.1 28.1 1.0 O C:ALA495 2.2 34.8 1.0 O C:HOH2936 2.2 34.2 1.0 O C:HOH2935 2.3 31.4 1.0 O C:HOH2937 2.3 33.4 1.0 CD C:GLU491 3.0 33.2 1.0 CG C:ASP454 3.1 38.3 1.0 C C:ALA495 3.3 35.1 1.0 OE2 C:GLU491 3.4 33.4 1.0 OD2 C:ASP454 3.5 32.0 1.0 N C:ALA495 3.9 29.6 1.0 O C:THR323 3.9 34.1 1.0 CA C:ALA495 4.1 37.5 1.0 N C:PHE496 4.2 31.0 1.0 CG C:GLU491 4.3 31.2 1.0 CA C:PHE496 4.3 29.7 1.0 CB C:ASP454 4.4 27.3 1.0 O C:HOH2270 4.4 54.9 1.0 CB C:GLU491 4.5 30.2 1.0 O C:ALA455 4.5 31.7 1.0 N C:ALA455 4.6 33.8 1.0 CB C:ALA495 4.6 36.6 1.0 O C:HOH2725 4.6 45.1 1.0 CA C:ASP454 4.7 32.8 1.0

S.J.Butcher, J.M.Grimes, E.V.Makeyev, D.H.Bamford, D.I.Stuart. A Mechanism For Initiating Rna-Dependent Rna Polymerization Nature V. 410 235 2001.
ISSN: ISSN 0028-0836
PubMed: 11242087
DOI: 10.1038/35065653