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Magnesium in PDB 1h78: Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp.

Enzymatic activity of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp.

All present enzymatic activity of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp.:
1.17.4.2;

Protein crystallography data

The structure of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp., PDB code: 1h78 was solved by K.-M.Larsson, J.Andersson, B.-M.Sjoeberg, P.Nordlund, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.935, 97.935, 242.515, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 25.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp. (pdb code 1h78). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp., PDB code: 1h78:

Magnesium binding site 1 out of 1 in 1h78

Go back to Magnesium Binding Sites List in 1h78
Magnesium binding site 1 out of 1 in the Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Allosteric Substrate Specificity Regulation in Class III Ribonucleotide Reductases: Nrdd in Complex with Dctp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1590

b:38.8
occ:1.00
 O1A A:DCP1589 1.8 60.5 1.0
O1G A:DCP1589 1.8 70.6 1.0
O2B A:DCP1589 2.1 56.9 1.0
O A:HOH2096 2.2 63.9 1.0
PG A:DCP1589 2.8 72.7 1.0
PB A:DCP1589 2.9 66.8 1.0
PA A:DCP1589 3.1 58.2 1.0
O3G A:DCP1589 3.2 73.8 1.0
O3B A:DCP1589 3.2 70.0 1.0
O3A A:DCP1589 3.4 58.9 1.0
O5' A:DCP1589 4.1 61.4 1.0
O2A A:DCP1589 4.2 60.0 1.0
O2G A:DCP1589 4.2 77.1 1.0
CG A:LYS103 4.4 65.7 1.0
C5' A:DCP1589 4.4 62.3 1.0
O1B A:DCP1589 4.4 56.4 1.0

Reference:

K.-M.Larsson, J.Andersson, B.-M.Sjoeberg, P.Nordlund, D.T.Logan. Structural Basis For Allosteric Substrate Specificty Regulation in Anaerobic Ribonucleotide Reductase Structure V. 9 739 2001.
ISSN: ISSN 0969-2126
PubMed: 11587648
DOI: 10.1016/S0969-2126(01)00627-X
Page generated: Tue Aug 13 03:53:30 2024

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