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

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

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp-Gdp Complex, PDB code: 1xje 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)	18.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.391, 124.376, 107.243, 90.00, 103.68, 90.00
R / Rfree (%)	18.2 / 22.3

The binding sites of Magnesium atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp-Gdp Complex (pdb code 1xje). 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-Gdp Complex, PDB code: 1xje:
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-Gdp 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-Gdp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1006 b:34.7 occ:1.00 O A:HOH1260 1.8 36.6 1.0 O2G A:TTP1005 1.9 36.5 1.0 O2B A:TTP1005 1.9 34.6 1.0 O1A A:TTP1005 2.0 28.5 1.0 O A:HOH1259 2.2 34.5 1.0 O A:HOH1271 2.4 41.9 1.0 PB A:TTP1005 3.0 35.7 1.0 PG A:TTP1005 3.1 38.0 1.0 PA A:TTP1005 3.2 29.9 1.0 O A:HOH1343 3.3 67.4 1.0 O3A A:TTP1005 3.4 31.4 1.0 O3B A:TTP1005 3.4 35.6 1.0 O3G A:TTP1005 3.5 39.2 1.0 O5' A:TTP1005 4.1 29.6 1.0 C5' A:TTP1005 4.1 25.9 1.0 NH2 A:ARG171 4.2 27.4 1.0 O2A A:TTP1005 4.2 27.4 1.0 O A:HOH1377 4.2 58.8 1.0 O A:HOH1272 4.3 54.5 1.0 O A:ASP141 4.3 25.5 1.0 O1B A:TTP1005 4.4 37.0 1.0 O1G A:TTP1005 4.4 32.8 1.0 O A:HOH1328 4.4 51.2 1.0 CB A:SER142 4.5 25.1 1.0 CA A:SER142 4.9 25.9 1.0

Magnesium binding site 2 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dttp-Gdp 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-Gdp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1007 b:41.8 occ:1.00 O2B B:TTP1004 1.8 49.3 1.0 O1A B:TTP1004 1.9 29.8 1.0 O2G B:TTP1004 3.0 60.6 1.0 PB B:TTP1004 3.1 54.1 1.0 PA B:TTP1004 3.2 33.4 1.0 O3A B:TTP1004 3.6 37.3 1.0 O2A B:TTP1004 3.9 30.5 1.0 PG B:TTP1004 3.9 59.7 1.0 CB B:SER142 4.0 29.2 1.0 O3B B:TTP1004 4.0 53.0 1.0 O3G B:TTP1004 4.0 56.6 1.0 O1B B:TTP1004 4.2 50.6 1.0 O5' B:TTP1004 4.3 30.4 1.0 NZ A:LYS158 4.5 33.9 1.0 C5' B:TTP1004 4.5 27.9 1.0 O B:ASP141 4.6 27.0 1.0 CA B:SER142 4.6 28.5 1.0 O B:HOH1365 4.8 30.4 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