Manganese in PDB 5j1p: Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions

All present enzymatic activity of Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions:
2.7.7.48;

The structure of Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions, PDB code: 5j1p was solved by J.Reguera, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.43 / 2.36
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	51.420, 51.420, 144.180, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 28.9

The binding sites of Manganese atom in the Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions (pdb code 5j1p). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions, PDB code: 5j1p:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:70.7 occ:1.00 OD1 A:ASP89 1.9 65.4 1.0 OE2 A:GLU51 2.4 60.6 1.0 CG A:ASP89 2.9 57.3 1.0 CD A:GLU51 3.3 63.4 1.0 OD2 A:ASP89 3.3 58.6 1.0 MN A:MN3202 3.5 70.6 1.0 CG A:GLU51 3.8 61.1 1.0 O A:HOH303 3.9 53.4 1.0 O A:CYS103 3.9 60.1 1.0 CB A:ASP89 4.2 56.9 1.0 OE1 A:GLU51 4.3 65.5 1.0 O A:HOH305 4.8 54.4 1.0 SG A:CYS103 4.9 62.5 1.0

Manganese binding site 2 out of 3 in the Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:70.6 occ:1.00 OE1 A:GLU102 1.9 81.7 1.0 OD2 A:ASP89 2.1 58.6 1.0 O A:HOH303 2.4 53.4 1.0 CD A:GLU102 2.9 77.9 1.0 CG A:ASP89 3.0 57.3 1.0 OD1 A:ASP89 3.3 65.4 1.0 OE2 A:GLU102 3.3 75.7 1.0 MN A:MN3201 3.5 70.7 1.0 O A:CYS103 3.8 60.1 1.0 CG A:GLU102 4.2 68.6 1.0 OD2 A:ASP119 4.3 68.5 1.0 CB A:ASP89 4.3 56.9 1.0 NZ A:LYS122 4.3 77.2 1.0 CB A:GLU102 4.4 58.5 1.0 N A:CYS103 4.4 56.1 1.0 CA A:GLU102 4.5 57.0 1.0 N A:ASP89 4.6 50.7 1.0 NZ A:LYS115 4.7 65.7 1.0 OD1 A:ASP119 4.9 63.5 1.0 C A:CYS103 4.9 60.1 1.0 C A:GLU102 4.9 59.5 1.0 CG A:ASP119 4.9 66.8 1.0 O A:VAL87 4.9 54.6 1.0 CA A:ASP89 5.0 55.1 1.0

Manganese binding site 3 out of 3 in the Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Lassa Virus L Protein Cap-Snatching Endonuclease. Bound to Two Manganese Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn203 b:91.3 occ:1.00 O A:HOH313 2.4 53.8 1.0 O A:HOH301 2.6 50.3 1.0 CE1 A:HIS76 2.7 99.2 1.0 NE2 A:HIS76 2.9 98.5 1.0 O A:LEU93 3.7 75.4 1.0 ND1 A:HIS76 4.0 97.0 1.0 CD2 A:HIS76 4.3 90.7 1.0 OE1 A:GLU61 4.3 91.7 0.0 OE2 A:GLU61 4.4 99.2 0.0 N A:LEU93 4.6 70.2 1.0 C A:LEU93 4.7 75.6 1.0 CD A:GLU61 4.7 90.1 0.0 CG A:HIS76 4.8 92.9 1.0 CB A:LEU93 4.8 72.7 1.0 CA A:LEU93 4.9 78.7 1.0

J.Reguera, P.Gerlach, M.Rosenthal, S.Gaudon, F.Coscia, S.Gunther, S.Cusack. Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases. Plos Pathog. V. 12 05636 2016.
ISSN: ESSN 1553-7374
PubMed: 27304209
DOI: 10.1371/JOURNAL.PPAT.1005636