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

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

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp Complex, PDB code: 1xjf 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)	22.88 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.300, 123.760, 107.030, 90.00, 103.82, 90.00
R / Rfree (%)	20.8 / 26

The binding sites of Magnesium atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp Complex (pdb code 1xjf). 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 Complex, PDB code: 1xjf:
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 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 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1004 b:50.8 occ:1.00 O2B A:DTP1002 1.8 63.1 1.0 O1A A:DTP1002 2.3 42.8 1.0 O2G A:DTP1002 3.0 67.2 1.0 PB A:DTP1002 3.3 64.5 1.0 PA A:DTP1002 3.6 47.8 1.0 CB A:SER142 3.9 41.8 1.0 O3A A:DTP1002 3.9 57.3 1.0 PG A:DTP1002 4.1 69.0 1.0 O3B A:DTP1002 4.2 66.2 1.0 O1B A:DTP1002 4.3 63.5 1.0 O A:ASP141 4.3 43.4 1.0 O3G A:DTP1002 4.4 69.1 1.0 O2A A:DTP1002 4.5 42.9 1.0 CA A:SER142 4.6 41.4 1.0 C5' A:DTP1002 4.7 34.5 1.0 O5' A:DTP1002 4.8 41.1 1.0 OG A:SER142 4.9 42.7 1.0

Magnesium binding site 2 out of 2 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp 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 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1003 b:48.4 occ:1.00 O2B B:DTP1001 1.2 62.1 1.0 O1A B:DTP1001 2.1 50.3 1.0 O2G B:DTP1001 2.4 67.8 1.0 PB B:DTP1001 2.7 68.1 1.0 PA B:DTP1001 3.4 49.4 1.0 PG B:DTP1001 3.5 69.2 1.0 O3B B:DTP1001 3.5 64.4 1.0 O3A B:DTP1001 3.6 59.7 1.0 O1B B:DTP1001 3.7 68.7 1.0 O3G B:DTP1001 4.0 68.2 1.0 CB B:SER142 4.0 41.8 1.0 O2A B:DTP1001 4.1 52.5 1.0 O B:ASP141 4.3 43.2 1.0 C5' B:DTP1001 4.6 42.4 1.0 O5' B:DTP1001 4.6 49.5 1.0 CA B:SER142 4.8 41.7 1.0 O1G B:DTP1001 4.8 68.4 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