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Magnesium in PDB 2a5f: Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6

Enzymatic activity of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6

All present enzymatic activity of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6:
2.4.2.36;

Protein crystallography data

The structure of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6, PDB code: 2a5f 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) 43.15 / 2.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.905, 90.925, 98.001, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.1

Other elements in 2a5f:

The structure of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6 also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6 (pdb code 2a5f). 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 Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6, PDB code: 2a5f:

Magnesium binding site 1 out of 1 in 2a5f

Go back to Magnesium Binding Sites List in 2a5f
Magnesium binding site 1 out of 1 in the Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg231

b:35.9
occ:1.00
 OG1 A:THR27 2.0 37.5 1.0
O2G A:GTP230 2.0 41.1 1.0
O A:HOH291 2.1 28.5 1.0
O A:HOH274 2.1 36.5 1.0
OG1 A:THR44 2.1 37.6 1.0
O2B A:GTP230 2.2 37.9 1.0
CB A:THR27 3.1 37.3 1.0
CB A:THR44 3.2 37.6 1.0
PG A:GTP230 3.2 45.9 1.0
PB A:GTP230 3.3 38.8 1.0
O3B A:GTP230 3.5 40.5 1.0
N A:THR44 3.7 37.8 1.0
O3G A:GTP230 3.9 41.1 1.0
N A:THR27 3.9 35.7 1.0
OD2 A:ASP63 4.0 36.2 1.0
OD1 A:ASP63 4.0 36.4 1.0
CA A:THR44 4.1 37.0 1.0
O2A A:GTP230 4.1 38.0 1.0
CA A:THR27 4.1 37.0 1.0
CG2 A:THR27 4.1 37.9 1.0
O A:HOH255 4.2 38.4 1.0
CG2 A:THR44 4.3 38.0 1.0
O A:ILE42 4.3 40.7 1.0
O1B A:GTP230 4.3 38.0 1.0
CG A:ASP63 4.4 35.5 1.0
O3A A:GTP230 4.4 38.4 1.0
O1G A:GTP230 4.5 43.6 1.0
PA A:GTP230 4.7 37.8 1.0
C A:PRO43 4.7 38.7 1.0
O1A A:GTP230 4.8 38.3 1.0
CB A:LYS26 4.9 35.1 1.0
CA A:PRO43 4.9 39.7 1.0
O A:HOH1108 5.0 55.5 1.0
NZ A:LYS26 5.0 34.3 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 20:22:45 2024

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