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Manganese in PDB 4wzm: Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna

Enzymatic activity of Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna

All present enzymatic activity of Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna:
2.7.7.48;

Protein crystallography data

The structure of Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna, PDB code: 4wzm was solved by N.Verdaguer, C.Ferrer-Orta, N.De La Higuera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.67 / 2.52
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 94.306, 94.306, 100.815, 90.00, 90.00, 120.00
R / Rfree (%) 22.4 / 26.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna (pdb code 4wzm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna, PDB code: 4wzm:

Manganese binding site 1 out of 1 in 4wzm

Go back to Manganese Binding Sites List in 4wzm
Manganese binding site 1 out of 1 in the Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mutant K18E of Rna Dependent Rna Polymerase From Foot-and-Mouth Disease Virus Complexed with Rna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn504

b:0.4
occ:1.00
OD1 A:ASP63 2.6 48.7 1.0
O A:THR64 2.7 53.7 1.0
N A:SER250 2.9 48.1 1.0
N A:ASP251 3.0 47.9 1.0
CB A:SER250 3.3 49.7 1.0
NZ A:LYS65 3.4 54.1 1.0
OD1 A:ASP251 3.4 52.4 1.0
CA A:SER250 3.4 47.4 1.0
CG A:ASP251 3.4 52.3 1.0
CG A:ASP63 3.5 48.9 1.0
CB A:CYS249 3.6 45.8 1.0
C A:SER250 3.6 47.7 1.0
C A:CYS249 3.7 46.5 1.0
OD2 A:ASP63 3.7 51.0 1.0
CE A:LYS65 3.8 54.0 1.0
OD2 A:ASP251 3.8 57.1 1.0
CD A:LYS65 3.8 53.0 1.0
C A:THR64 3.9 51.0 1.0
CB A:ASP251 3.9 51.1 1.0
CA A:CYS249 4.0 44.5 1.0
CA A:ASP251 4.0 49.4 1.0
SG A:CYS249 4.0 49.0 1.0
O A:ASP63 4.2 48.7 1.0
OG A:SER250 4.2 51.4 1.0
CA A:LYS65 4.4 51.4 1.0
C A:ASP63 4.5 48.6 1.0
O A:CYS249 4.5 45.8 1.0
N A:LYS65 4.5 51.4 1.0
CB A:ASP63 4.7 48.9 1.0
O A:SER250 4.8 49.6 1.0
N A:THR64 4.8 48.3 1.0
CA A:THR64 4.9 48.5 1.0
CG A:LYS65 5.0 53.0 1.0

Reference:

C.Ferrer-Orta, I.De La Higuera, F.Caridi, M.T.Sanchez-Aparicio, E.Moreno, C.Perales, K.Singh, S.G.Sarafianos, F.Sobrino, E.Domingo, N.Verdaguer. Multifunctionality of A Picornavirus Polymerase Domain: Nuclear Localization Signal and Nucleotide Recognition. J.Virol. 2015.
ISSN: ESSN 1098-5514
PubMed: 25903341
DOI: 10.1128/JVI.03283-14
Page generated: Tue Dec 15 04:33:13 2020

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