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Magnesium in PDB 3tra: Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals

Protein crystallography data

The structure of Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals, PDB code: 3tra was solved by E.Westhof, P.Dumas, D.Moras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 3.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 60.300, 68.000, 149.500, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals (pdb code 3tra). 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 Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals, PDB code: 3tra:

Magnesium binding site 1 out of 1 in 3tra

Go back to Magnesium Binding Sites List in 3tra
Magnesium binding site 1 out of 1 in the Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg76

b:34.6
occ:0.81
N4 A:C31 3.9 11.5 1.0
O A:HOH133 4.0 33.9 0.9
OP2 A:1MG37 4.1 36.5 1.0
O2 A:PSU32 4.3 14.8 1.0
OP1 A:1MG37 4.4 33.1 1.0
P A:1MG37 4.8 37.7 1.0

Reference:

E.Westhof, P.Dumas, D.Moras. Restrained Refinement of Two Crystalline Forms of Yeast Aspartic Acid and Phenylalanine Transfer Rna Crystals. Acta Crystallogr.,Sect.A V. 44 112 1988.
ISSN: ISSN 0108-7673
PubMed: 3272146
DOI: 10.1107/S010876738700446X
Page generated: Mon Dec 14 08:54:54 2020

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