Magnesium in PDB 3s8c: Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp

All present enzymatic activity of Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp:
1.17.4.1;

The structure of Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp, PDB code: 3s8c was solved by M.F.Ahmad, P.S.Kaushal, Q.Wan, S.R.Wijeratna, M.Huang, C.D.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.29 / 2.77
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.781, 116.810, 64.126, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 25.6

The binding sites of Magnesium atom in the Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp (pdb code 3s8c). 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 Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp, PDB code: 3s8c:

Magnesium binding site 1 out of 1 in the Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Yeast Ribonucleotide Reductase 1 R293A with Amppnp and Cdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg890 b:67.6 occ:1.00 O1A A:ANP889 2.3 58.7 1.0 O A:HOH911 2.4 45.7 1.0 O2B A:ANP889 2.5 59.0 1.0 O3G A:ANP889 3.5 62.4 1.0 PA A:ANP889 3.6 60.8 1.0 CB A:SER227 3.7 40.9 1.0 PB A:ANP889 3.8 60.8 1.0 O3A A:ANP889 4.3 60.4 1.0 O A:ASP226 4.3 42.4 1.0 O2G A:ANP889 4.3 63.5 1.0 O2A A:ANP889 4.4 59.7 1.0 PG A:ANP889 4.4 62.7 1.0 CA A:SER227 4.6 41.1 1.0 N3B A:ANP889 4.7 61.0 1.0 OG A:SER227 4.7 40.0 1.0 O5' A:ANP889 4.8 55.4 1.0 O A:HOH914 4.8 35.3 1.0 C5' A:ANP889 4.9 54.1 1.0

M.F.Ahmad, P.S.Kaushal, Q.Wan, S.R.Wijeratna, M.Huang, C.D.Dealwis. Structural and Biochemical Basis of Lethal Mutant R293A of Yeast Ribonucleotide Reductase To Be Published.