Magnesium in PDB 1xjm: Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex

All present enzymatic activity of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex:
1.17.4.1;

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex, PDB code: 1xjm was solved by K.-M.Larsson, A.Jordan, R.Eliasson, P.Reichard, D.T.Logan, P.Nordlund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.438, 123.776, 106.241, 90.00, 103.64, 90.00
R / Rfree (%)	18.4 / 24.7

The binding sites of Magnesium atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex (pdb code 1xjm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex, PDB code: 1xjm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1005 b:38.1 occ:1.00 O2B A:TTP1001 2.2 38.4 1.0 O1A A:TTP1001 2.2 27.1 1.0 O2G A:TTP1001 2.5 42.2 1.0 PB A:TTP1001 3.3 42.2 1.0 PA A:TTP1001 3.4 28.2 1.0 PG A:TTP1001 3.6 46.8 1.0 O3A A:TTP1001 3.8 33.9 1.0 O3G A:TTP1001 3.9 43.2 1.0 O3B A:TTP1001 4.0 41.4 1.0 CB A:SER142 4.2 26.8 1.0 O2A A:TTP1001 4.2 28.7 1.0 O A:ASP141 4.5 27.8 1.0 O5' A:TTP1001 4.6 26.6 1.0 O1B A:TTP1001 4.7 42.6 1.0 C5' A:TTP1001 4.7 25.3 1.0 CA A:SER142 4.9 27.2 1.0 O A:HOH1039 5.0 25.5 1.0 NH2 A:ARG171 5.0 21.9 1.0 NZ B:LYS158 5.0 33.3 1.0

Magnesium binding site 2 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1006 b:28.0 occ:1.00 O2B B:TTP1002 1.7 58.8 1.0 O1A B:TTP1002 1.8 38.2 1.0 O B:HOH1112 2.9 52.9 1.0 PB B:TTP1002 3.0 63.1 1.0 PA B:TTP1002 3.0 37.9 1.0 O3A B:TTP1002 3.5 48.3 1.0 O2A B:TTP1002 3.6 36.7 1.0 O3G B:TTP1002 3.7 67.5 1.0 CB B:SER142 3.7 26.9 1.0 O1B B:TTP1002 3.9 58.7 1.0 NZ A:LYS158 4.1 37.9 1.0 O3B B:TTP1002 4.1 64.6 1.0 O5' B:TTP1002 4.2 36.4 1.0 O2G B:TTP1002 4.3 70.7 1.0 PG B:TTP1002 4.4 68.4 1.0 O B:HOH1062 4.4 24.7 1.0 CA B:SER142 4.4 26.7 1.0 C5' B:TTP1002 4.4 31.8 1.0 O B:ASP141 4.5 28.1 1.0 OG B:SER142 4.9 27.1 1.0

K.-M.Larsson, A.Jordan, R.Eliasson, P.Reichard, D.T.Logan, P.Nordlund. Structural Mechanism of Allosteric Substrate Specificity Regulation in A Ribonucleotide Reductase. Nat.Struct.Mol.Biol. V. 11 1142 2004.
ISSN: ISSN 1545-9993
PubMed: 15475969
DOI: 10.1038/NSMB838