Magnesium in PDB 1xjg: Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Udp Complex

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

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Udp Complex, PDB code: 1xjg 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)	24.87 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.537, 123.514, 105.886, 90.00, 102.60, 90.00
R / Rfree (%)	19.5 / 26.4

The binding sites of Magnesium atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Udp Complex (pdb code 1xjg). 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: Datp-Udp Complex, PDB code: 1xjg:
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: Datp-Udp 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: Datp-Udp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1006 b:58.4 occ:1.00 O2B A:DTP1004 1.9 55.5 1.0 O1A A:DTP1004 2.7 48.9 1.0 PB A:DTP1004 3.2 57.8 1.0 CB A:SER142 3.7 51.5 1.0 O2G A:DTP1004 3.8 58.3 1.0 O1B A:DTP1004 3.8 56.5 1.0 PA A:DTP1004 3.9 54.7 1.0 O3A A:DTP1004 4.1 58.1 1.0 O3B A:DTP1004 4.4 58.3 1.0 CA A:SER142 4.5 52.4 1.0 O A:ASP141 4.5 52.4 1.0 OG A:SER142 4.6 49.4 1.0 PG A:DTP1004 4.6 57.0 1.0 O2A A:DTP1004 4.6 54.3 1.0 O A:SER142 4.7 55.4 1.0 O3G A:DTP1004 4.7 56.4 1.0

Magnesium binding site 2 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Udp 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: Datp-Udp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1005 b:71.3 occ:1.00 O2B B:DTP1003 1.3 54.9 1.0 O1A B:DTP1003 2.1 48.8 1.0 O2G B:DTP1003 2.2 67.4 1.0 PB B:DTP1003 2.6 63.1 1.0 PA B:DTP1003 3.2 53.9 1.0 O3A B:DTP1003 3.3 60.3 1.0 PG B:DTP1003 3.4 68.4 1.0 O3B B:DTP1003 3.4 62.8 1.0 O1B B:DTP1003 3.8 62.5 1.0 O B:ASP141 3.9 45.5 1.0 CB B:SER142 4.0 45.3 1.0 O2A B:DTP1003 4.2 51.7 1.0 C5' B:DTP1003 4.3 51.0 1.0 O5' B:DTP1003 4.3 52.6 1.0 O3G B:DTP1003 4.3 63.5 1.0 O1G B:DTP1003 4.4 66.1 1.0 CA B:SER142 4.5 45.2 1.0 NH2 B:ARG171 4.8 40.1 1.0 C B:ASP141 4.8 45.5 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