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Magnesium in PDB 1kuv: X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition

Enzymatic activity of X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition

All present enzymatic activity of X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition:
2.3.1.87;

Protein crystallography data

The structure of X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition, PDB code: 1kuv was solved by E.Wolf, J.De Angelis, E.M.Khalil, P.A.Cole, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.313, 68.716, 89.725, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 25

Other elements in 1kuv:

The structure of X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition also contains other interesting chemical elements:

Bromine (Br) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition (pdb code 1kuv). 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 X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition, PDB code: 1kuv:

Magnesium binding site 1 out of 1 in 1kuv

Go back to Magnesium Binding Sites List in 1kuv
Magnesium binding site 1 out of 1 in the X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition within 5.0Å range:

Reference:

E.Wolf, J.De Angelis, E.M.Khalil, P.A.Cole, S.K.Burley. X-Ray Crystallographic Studies of Serotonin N-Acetyltransferase Catalysis and Inhibition. J.Mol.Biol. V. 317 215 2002.
ISSN: ISSN 0022-2836
PubMed: 11902838
DOI: 10.1006/JMBI.2001.5371
Page generated: Tue Aug 13 08:09:08 2024

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