Magnesium in PDB 5tus: Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule

All present enzymatic activity of Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule:
1.17.4.1;

The structure of Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule, PDB code: 5tus was solved by F.A.Mohammed, I.Alam, C.G.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	110.18 / 2.66
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.516, 114.282, 220.361, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 25

The binding sites of Magnesium atom in the Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule (pdb code 5tus). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule, PDB code: 5tus:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1602 b:46.9 occ:1.00 O3B A:TTP1601 1.9 69.4 1.0 O1A A:TTP1601 2.2 57.5 1.0 O2B A:TTP1601 2.5 69.6 1.0 PB A:TTP1601 2.8 79.4 1.0 O3G A:TTP1601 2.9 80.1 1.0 PG A:TTP1601 3.1 65.2 1.0 PA A:TTP1601 3.4 55.3 1.0 O3A A:TTP1601 3.6 61.5 1.0 O1G A:TTP1601 3.7 72.2 1.0 CB A:SER227 4.0 43.0 1.0 O1B A:TTP1601 4.1 69.8 1.0 O2A A:TTP1601 4.2 51.5 1.0 O2G A:TTP1601 4.3 61.3 1.0 O5' A:TTP1601 4.6 56.9 1.0 O A:ASP226 4.6 49.5 1.0 C5' A:TTP1601 4.7 50.9 1.0 CA A:SER227 4.9 44.6 1.0 NH2 A:ARG256 5.0 51.9 1.0

Magnesium binding site 2 out of 2 in the Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Novel Non-Nucleoside Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1602 b:45.8 occ:1.00 O2B B:TTP1601 1.7 75.1 1.0 O1G B:TTP1601 1.8 58.7 1.0 O2A B:TTP1601 2.1 52.9 1.0 PB B:TTP1601 2.8 94.1 1.0 PG B:TTP1601 3.0 69.9 1.0 O3B B:TTP1601 3.3 77.6 1.0 PA B:TTP1601 3.3 51.8 1.0 O3A B:TTP1601 3.5 75.0 1.0 O2G B:TTP1601 3.6 71.7 1.0 CB B:SER227 4.0 43.6 1.0 O1A B:TTP1601 4.2 50.7 1.0 O1B B:TTP1601 4.2 87.3 1.0 NH2 B:ARG256 4.2 68.3 1.0 O3G B:TTP1601 4.4 56.3 1.0 O B:ASP226 4.5 53.6 1.0 O5' B:TTP1601 4.5 53.3 1.0 CA B:SER227 4.6 47.0 1.0 C5' B:TTP1601 4.7 54.5 1.0 NZ A:LYS243 4.9 70.4 1.0

M.F.Ahmad, I.Alam, S.E.Huff, J.Pink, S.A.Flanagan, D.Shewach, T.A.Misko, N.L.Oleinick, W.E.Harte, R.Viswanathan, M.E.Harris, C.G.Dealwis. Potent Competitive Inhibition of Human Ribonucleotide Reductase By A Nonnucleoside Small Molecule. Proc. Natl. Acad. Sci. V. 114 8241 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28716944
DOI: 10.1073/PNAS.1620220114