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Magnesium in PDB 2a5d: Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp

Enzymatic activity of Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp

All present enzymatic activity of Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp:
2.4.2.36;

Protein crystallography data

The structure of Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp, PDB code: 2a5d was solved by C.J.O'neal, M.G.Jobling, R.K.Holmes, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.74 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.915, 91.446, 98.547, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 19.9

Other elements in 2a5d:

The structure of Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp (pdb code 2a5d). 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 Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp, PDB code: 2a5d:

Magnesium binding site 1 out of 1 in 2a5d

Go back to Magnesium Binding Sites List in 2a5d
Magnesium binding site 1 out of 1 in the Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1231

b:6.8
occ:1.00
 O A:HOH1233 2.0 9.7 1.0
OG1 A:THR27 2.0 19.4 1.0
O2B A:GTP1230 2.0 8.3 1.0
O2G A:GTP1230 2.0 7.2 1.0
OG1 A:THR44 2.1 18.0 1.0
O A:HOH1232 2.1 2.6 1.0
CB A:THR27 3.1 21.1 1.0
CB A:THR44 3.1 20.6 1.0
PG A:GTP1230 3.2 12.8 1.0
PB A:GTP1230 3.3 8.1 1.0
O3B A:GTP1230 3.5 9.1 1.0
O3G A:GTP1230 3.7 12.2 1.0
N A:THR44 3.8 20.9 1.0
N A:THR27 3.9 19.8 1.0
OD1 A:ASP63 4.0 24.3 1.0
OD2 A:ASP63 4.1 22.0 1.0
CA A:THR27 4.1 20.1 1.0
CA A:THR44 4.1 19.8 1.0
CG2 A:THR27 4.1 21.1 1.0
O A:HOH203 4.2 12.1 1.0
O2A A:GTP1230 4.2 9.2 1.0
CG2 A:THR44 4.2 20.6 1.0
O A:ILE42 4.3 21.6 1.0
O3A A:GTP1230 4.3 8.7 1.0
O1B A:GTP1230 4.4 6.8 1.0
O1G A:GTP1230 4.5 12.2 1.0
CG A:ASP63 4.5 21.4 1.0
PA A:GTP1230 4.6 9.6 1.0
O1A A:GTP1230 4.7 9.4 1.0
C A:PRO43 4.8 20.3 1.0
OD1 A:ASN48 4.8 26.0 1.0
CA A:PRO43 4.9 19.9 1.0
CB A:LYS26 4.9 22.2 1.0

Reference:

C.J.O'neal, M.G.Jobling, R.K.Holmes, W.G.Hol. Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp. Science V. 309 1093 2005.
ISSN: ISSN 0036-8075
PubMed: 16099990
DOI: 10.1126/SCIENCE.1113398
Page generated: Tue Aug 13 20:22:42 2024

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