Magnesium in PDB 3hnc: Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effector Ttp

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

The structure of Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effector Ttp, PDB code: 3hnc 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)	39.53 / 2.41
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.980, 114.104, 219.283, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.6

The binding sites of Magnesium atom in the Crystal Structure of Human Ribonucleotide Reductase 1 Bound to the Effector Ttp (pdb code 3hnc). 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 Effector Ttp, PDB code: 3hnc:
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 Effector Ttp


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 Effector Ttp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:52.2 occ:1.00 O2A A:TTP802 1.9 43.3 1.0 O A:HOH921 2.2 43.2 1.0 O2B A:TTP802 2.2 47.5 1.0 O3G A:TTP802 2.5 49.0 1.0 PA A:TTP802 3.2 43.1 1.0 PB A:TTP802 3.3 49.0 1.0 PG A:TTP802 3.6 49.7 1.0 O3A A:TTP802 3.7 46.5 1.0 CB A:SER227 3.7 45.9 1.0 O3B A:TTP802 3.9 48.2 1.0 O1A A:TTP802 3.9 41.6 1.0 O A:ASP226 4.0 48.9 1.0 O1G A:TTP802 4.1 50.0 1.0 NH1 A:ARG256 4.2 42.6 1.0 O5' A:TTP802 4.4 42.7 1.0 CA A:SER227 4.4 45.6 1.0 C5' A:TTP802 4.5 41.8 1.0 O1B A:TTP802 4.6 48.2 1.0 OG A:SER227 4.9 44.9 1.0 O2G A:TTP802 4.9 48.2 1.0 C A:ASP226 4.9 47.8 1.0

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


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 Effector Ttp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg801 b:50.4 occ:1.00 O2A B:TTP802 2.0 46.1 1.0 O2B B:TTP802 2.0 50.9 1.0 O B:HOH919 2.2 39.4 1.0 O3G B:TTP802 2.5 54.9 1.0 PB B:TTP802 3.2 53.0 1.0 PA B:TTP802 3.3 45.6 1.0 PG B:TTP802 3.3 54.5 1.0 O1G B:TTP802 3.4 55.8 1.0 O3A B:TTP802 3.6 49.7 1.0 O3B B:TTP802 3.7 53.0 1.0 CB B:SER227 4.1 48.3 1.0 O1A B:TTP802 4.2 44.6 1.0 O B:ASP226 4.2 48.4 1.0 O1B B:TTP802 4.5 53.2 1.0 O5' B:TTP802 4.5 45.0 1.0 C5' B:TTP802 4.5 41.9 1.0 NH1 B:ARG256 4.7 42.1 1.0 O2G B:TTP802 4.8 53.3 1.0 CA B:SER227 4.8 48.1 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