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Magnesium in PDB 2v1u: Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna

Protein crystallography data

The structure of Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna, PDB code: 2v1u was solved by M.Gaudier, B.S.Schuwirth, S.L.Westcott, D.B.Wigley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 3.10
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 75.700, 75.700, 395.110, 90.00, 90.00, 120.00
R / Rfree (%) 25.4 / 29.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna (pdb code 2v1u). 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 Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna, PDB code: 2v1u:

Magnesium binding site 1 out of 1 in 2v1u

Go back to Magnesium Binding Sites List in 2v1u
Magnesium binding site 1 out of 1 in the Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Aeropyrum Pernix ORC1 Protein in Complex with Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1401

b:79.2
occ:1.00
OG1 A:THR70 2.2 0.1 1.0
O3B A:ADP1400 2.6 92.9 1.0
O1B A:ADP1400 2.7 84.0 1.0
PB A:ADP1400 3.1 0.5 1.0
CB A:THR70 3.3 0.2 1.0
O1A A:ADP1400 3.9 67.0 1.0
OE2 A:GLU150 3.9 0.4 1.0
O3A A:ADP1400 3.9 88.2 1.0
OD2 A:ASP149 4.0 92.2 1.0
CG2 A:THR70 4.1 0.5 1.0
NZ A:LYS69 4.2 0.7 1.0
O2B A:ADP1400 4.5 71.8 1.0
PA A:ADP1400 4.5 99.8 1.0
N A:THR70 4.5 94.7 1.0
CA A:THR70 4.5 99.8 1.0
OD1 A:ASP149 4.6 0.5 1.0
CD A:GLU150 4.6 0.1 1.0
CG A:ASP149 4.7 0.5 1.0

Reference:

M.Gaudier, B.S.Schuwirth, S.L.Westcott, D.B.Wigley. Structural Basis of Dna Replication Origin Recognition By An Orc Protein. Science V. 317 1213 2007.
ISSN: ISSN 0036-8075
PubMed: 17761880
DOI: 10.1126/SCIENCE.1143664
Page generated: Mon Dec 14 07:40:44 2020

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