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Magnesium in PDB 2cvt: Structures of Yeast Ribonucleotide Reductase I

Enzymatic activity of Structures of Yeast Ribonucleotide Reductase I

All present enzymatic activity of Structures of Yeast Ribonucleotide Reductase I:
1.17.4.1;

Protein crystallography data

The structure of Structures of Yeast Ribonucleotide Reductase I, PDB code: 2cvt was solved by H.Xu, C.Faber, T.Uchiki, J.W.Fairman, J.Racca, C.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.253, 117.071, 63.337, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 29.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structures of Yeast Ribonucleotide Reductase I (pdb code 2cvt). 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 Structures of Yeast Ribonucleotide Reductase I, PDB code: 2cvt:

Magnesium binding site 1 out of 1 in 2cvt

Go back to Magnesium Binding Sites List in 2cvt
Magnesium binding site 1 out of 1 in the Structures of Yeast Ribonucleotide Reductase I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structures of Yeast Ribonucleotide Reductase I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg889

b:67.8
occ:1.00
O3G A:ANP890 2.1 94.2 1.0
O3A A:ANP890 2.5 97.1 1.0
O5' A:ANP890 3.3 91.1 1.0
PA A:ANP890 3.3 93.3 1.0
PG A:ANP890 3.3 95.1 1.0
N3B A:ANP890 3.3 98.8 1.0
O2A A:ANP890 3.4 94.7 1.0
PB A:ANP890 3.6 0.9 1.0
CB A:SER227 4.0 64.6 1.0
NH2 A:ARG256 4.0 72.5 1.0
O1G A:ANP890 4.0 95.8 1.0
O1B A:ANP890 4.3 0.7 1.0
CA A:SER227 4.3 64.4 1.0
O A:ASP226 4.4 67.5 1.0
C5' A:ANP890 4.5 89.7 1.0
O2G A:ANP890 4.5 92.4 1.0
O1A A:ANP890 4.7 91.5 1.0
O2B A:ANP890 4.8 0.5 1.0

Reference:

H.Xu, C.Faber, T.Uchiki, J.W.Fairman, J.Racca, C.Dealwis. Structures of Eukaryotic Ribonucleotide Reductase I Provide Insights Into Dntp Regulation Proc.Natl.Acad.Sci.Usa V. 103 4022 2006.
ISSN: ISSN 0027-8424
PubMed: 16537479
DOI: 10.1073/PNAS.0600443103
Page generated: Tue Aug 13 22:21:41 2024

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