Magnesium in PDB 1xjk: Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dgtp-Adp Complex

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

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dgtp-Adp Complex, PDB code: 1xjk 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)	22.70 / 2.12
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.120, 122.860, 106.060, 90.00, 103.46, 90.00
R / Rfree (%)	20.5 / 25.6

The binding sites of Magnesium atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dgtp-Adp Complex (pdb code 1xjk). 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: Dgtp-Adp Complex, PDB code: 1xjk:
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: Dgtp-Adp 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: Dgtp-Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1005 b:46.5 occ:1.00 O1A A:DGT1003 1.9 35.9 1.0 O2B A:DGT1003 2.2 40.7 1.0 O2G A:DGT1003 2.2 52.8 1.0 O A:HOH1105 2.3 31.9 1.0 PA A:DGT1003 3.1 38.4 1.0 PB A:DGT1003 3.2 43.8 1.0 PG A:DGT1003 3.2 49.3 1.0 O3G A:DGT1003 3.3 49.0 1.0 O3A A:DGT1003 3.4 41.2 1.0 O3B A:DGT1003 3.7 46.6 1.0 O5' A:DGT1003 4.1 35.6 1.0 CB A:SER142 4.2 36.0 1.0 C5' A:DGT1003 4.2 35.5 1.0 NH2 A:ARG171 4.2 37.1 1.0 O2A A:DGT1003 4.2 35.0 1.0 O A:ASP141 4.2 36.6 1.0 O A:HOH1124 4.3 60.8 1.0 O1G A:DGT1003 4.6 46.2 1.0 O1B A:DGT1003 4.6 43.6 1.0 O A:HOH1064 4.7 40.8 1.0 CA A:SER142 4.8 35.7 1.0

Magnesium binding site 2 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Dgtp-Adp 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: Dgtp-Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1006 b:44.9 occ:1.00 O1A B:DGT1004 1.8 36.3 1.0 O B:HOH1083 2.0 62.4 1.0 O2B B:DGT1004 2.1 48.0 1.0 O B:HOH1057 2.2 38.0 1.0 O2G B:DGT1004 2.5 51.5 1.0 PA B:DGT1004 3.2 39.4 1.0 PB B:DGT1004 3.3 52.1 1.0 PG B:DGT1004 3.6 52.9 1.0 O3A B:DGT1004 3.6 44.1 1.0 O3G B:DGT1004 3.7 48.4 1.0 O3B B:DGT1004 3.9 49.4 1.0 CB B:SER142 4.0 32.6 1.0 O2A B:DGT1004 4.1 39.6 1.0 O B:ASP141 4.2 37.3 1.0 O5' B:DGT1004 4.3 37.2 1.0 C5' B:DGT1004 4.3 35.2 1.0 O1B B:DGT1004 4.6 50.3 1.0 CA B:SER142 4.6 33.1 1.0 NH2 B:ARG171 4.9 41.1 1.0 O1G B:DGT1004 4.9 52.6 1.0 O B:HOH1086 5.0 36.8 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