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Magnesium in PDB 2oqx: Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution

Enzymatic activity of Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution

All present enzymatic activity of Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution:
4.1.99.1;

Protein crystallography data

The structure of Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution, PDB code: 2oqx was solved by Y.Goldgur, A.Kogan, G.Gdalevsky, A.Parola, R.Cohen-Luria, O.Almog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.82 / 1.90
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 118.422, 120.116, 171.209, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 23.2

Other elements in 2oqx:

The structure of Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution (pdb code 2oqx). 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 the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution, PDB code: 2oqx:

Magnesium binding site 1 out of 1 in 2oqx

Go back to Magnesium Binding Sites List in 2oqx
Magnesium binding site 1 out of 1 in the Crystal Structure of the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution


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 the Apo Form of E. Coli Tryptophanase at 1.9 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:17.5
occ:1.00
O A:HOH1044 2.0 13.7 1.0
O A:HOH1086 2.0 19.4 1.0
O A:HOH1079 2.1 24.7 1.0
O A:HOH1232 2.1 18.8 1.0
O A:HOH1025 2.1 18.5 1.0
O A:HOH1231 2.1 19.0 1.0
O A:HOH1016 4.0 22.3 1.0
O A:PRO275 4.0 24.7 1.0
O A:GLY55 4.3 15.5 1.0
O A:HOH1080 4.4 43.1 1.0
O A:SER54 4.7 16.5 1.0
O A:HOH1136 4.8 30.4 1.0
C A:GLY55 4.9 16.6 1.0

Reference:

N.Tsesin, A.Kogan, G.Y.Gdalevsky, J.P.Himanen, R.Cohen-Luria, A.H.Parola, Y.Goldgur, O.Almog. The Structure of Apo Tryptophanase From Escherichia Coli Reveals A Wide-Open Conformation. Acta Crystallogr.,Sect.D V. 63 969 2007.
ISSN: ISSN 0907-4449
PubMed: 17704565
DOI: 10.1107/S0907444907036396
Page generated: Wed Aug 14 01:33:09 2024

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