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Magnesium in PDB 2v0y: Crystal Structure of Apo C298S Tryptophanase From E.Coli

Enzymatic activity of Crystal Structure of Apo C298S Tryptophanase From E.Coli

All present enzymatic activity of Crystal Structure of Apo C298S Tryptophanase From E.Coli:
4.1.99.1;

Protein crystallography data

The structure of Crystal Structure of Apo C298S Tryptophanase From E.Coli, PDB code: 2v0y was solved by A.Kogan, G.Y.Gdalevsky, R.Cohen-Luria, Y.Goldgur, A.H.Parola, O.Almog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.00 / 2.00
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 120.484, 118.770, 171.534, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 25.7

Other elements in 2v0y:

The structure of Crystal Structure of Apo C298S Tryptophanase From E.Coli also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Apo C298S Tryptophanase From E.Coli (pdb code 2v0y). 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 Crystal Structure of Apo C298S Tryptophanase From E.Coli, PDB code: 2v0y:

Magnesium binding site 1 out of 1 in 2v0y

Go back to Magnesium Binding Sites List in 2v0y
Magnesium binding site 1 out of 1 in the Crystal Structure of Apo C298S Tryptophanase From E.Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Apo C298S Tryptophanase From E.Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1474

b:29.7
occ:1.00
O A:HOH2350 2.2 18.4 1.0
O A:HOH2105 2.3 28.7 1.0
O A:PRO275 4.0 25.5 1.0
O A:HOH2108 4.2 25.3 1.0
O A:GLY55 4.5 16.1 1.0
O A:SER54 4.9 17.8 1.0
C A:GLY55 5.0 16.7 1.0

Reference:

A.Kogan, G.Y.Gdalevsky, R.Cohen-Luria, Y.Goldgur, R.S.Phillips, A.H.Parola, O.Almog. Conformational Changes and Loose Packing Promote E. Coli Tryptophanase Cold Lability. Bmc Struct.Biol. V. 9 65 2009.
ISSN: ESSN 1472-6807
PubMed: 19814824
DOI: 10.1186/1472-6807-9-65
Page generated: Wed Aug 14 04:56:57 2024

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