Magnesium in PDB 3hnf: Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp

All present enzymatic activity of Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp:
1.17.4.1;

The structure of Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp, PDB code: 3hnf was solved by J.W.Fairman, S.R.Wijerathna, H.Xu, C.G.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.86 / 3.16
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.856, 114.388, 220.003, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 26

The binding sites of Magnesium atom in the Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp (pdb code 3hnf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp, PDB code: 3hnf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:47.0 occ:1.00 O2B A:TTP804 2.2 65.9 1.0 O2A A:TTP804 2.5 65.8 1.0 O3G A:TTP804 2.8 64.1 1.0 O1G A:TTP804 3.0 64.7 1.0 PB A:TTP804 3.3 67.0 1.0 PG A:TTP804 3.3 65.3 1.0 PA A:TTP804 3.5 65.3 1.0 O3A A:TTP804 3.7 66.7 1.0 O3B A:TTP804 3.7 66.3 1.0 O5' A:TTP804 3.8 63.7 1.0 NH1 A:ARG256 4.0 51.1 1.0 CB A:SER227 4.1 56.0 1.0 O A:ASP226 4.1 58.3 1.0 O1B A:TTP804 4.6 67.6 1.0 CA A:SER227 4.6 55.5 1.0 O2G A:TTP804 4.8 64.7 1.0 C5' A:TTP804 4.8 62.3 1.0 O1A A:TTP804 4.8 64.7 1.0 C A:ASP226 5.0 57.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effectors Ttp and Datp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:48.5 occ:1.00 O3G B:TTP803 2.4 66.1 1.0 O3B B:TTP803 2.4 65.1 1.0 O2A B:TTP803 2.5 54.6 1.0 PG B:TTP803 2.7 66.8 1.0 O2B B:TTP803 2.9 63.8 1.0 O1G B:TTP803 3.0 67.0 1.0 PB B:TTP803 3.2 64.2 1.0 PA B:TTP803 3.6 55.8 1.0 O B:ASP226 3.7 57.3 1.0 O3A B:TTP803 4.0 60.4 1.0 O5' B:TTP803 4.1 55.0 1.0 O2G B:TTP803 4.1 64.6 1.0 C5' B:TTP803 4.4 54.9 1.0 O1B B:TTP803 4.5 64.1 1.0 NH1 B:ARG256 4.5 47.1 1.0 CB B:SER227 4.7 57.7 1.0 C B:ASP226 4.9 56.4 1.0 O1A B:TTP803 4.9 56.2 1.0

J.W.Fairman, S.R.Wijerathna, M.F.Ahmad, H.Xu, R.Nakano, S.Jha, J.Prendergast, R.M.Welin, S.Flodin, A.Roos, P.Nordlund, Z.Li, T.Walz, C.G.Dealwis. Structural Basis For Allosteric Regulation of Human Ribonucleotide Reductase By Nucleotide-Induced Oligomerization. Nat.Struct.Mol.Biol. V. 18 316 2011.
ISSN: ISSN 1545-9993
PubMed: 21336276
DOI: 10.1038/NSMB.2007