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Sodium in PDB 3pzb: Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate

Enzymatic activity of Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate

All present enzymatic activity of Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate:
1.2.1.11;

Protein crystallography data

The structure of Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate, PDB code: 3pzb was solved by A.G.Pavlovsky, R.E.Viola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.042, 100.090, 64.483, 90.00, 100.81, 90.00
R / Rfree (%) 17.7 / 20.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate (pdb code 3pzb). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate, PDB code: 3pzb:

Sodium binding site 1 out of 1 in 3pzb

Go back to Sodium Binding Sites List in 3pzb
Sodium binding site 1 out of 1 in the Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystals Structure of Aspartate Beta-Semialdehyde Dehydrogenase Complex with Nadp and D-2,3-Diaminopropionate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na369

b:23.5
occ:1.00
O A:ALA279 2.3 16.4 1.0
O A:HOH483 2.3 20.6 1.0
O A:PHE276 2.4 16.0 1.0
O A:ALA274 2.4 17.6 1.0
C A:PHE276 3.3 16.3 1.0
C A:ALA274 3.4 17.5 1.0
C A:ALA279 3.5 16.3 1.0
N A:PHE276 3.6 16.9 1.0
O A:ILE273 3.7 16.1 1.0
O A:HOH394 3.9 26.5 1.0
C A:ALA275 3.9 17.5 1.0
N A:ALA279 4.0 15.9 1.0
CA A:PHE276 4.0 16.7 1.0
O A:HOH502 4.2 20.0 1.0
N A:ALA275 4.2 17.8 1.0
CA A:ALA279 4.2 16.0 1.0
CA A:ALA274 4.2 17.2 1.0
N A:PRO277 4.2 16.4 1.0
CA A:ALA275 4.3 17.9 1.0
CA A:PRO277 4.4 16.2 1.0
O A:ALA275 4.4 17.6 1.0
N A:VAL280 4.5 16.2 1.0
CB A:ALA279 4.5 16.2 1.0
N A:GLY278 4.6 15.9 1.0
CA A:VAL280 4.7 16.8 1.0
C A:ILE273 4.7 16.4 1.0
C A:PRO277 4.7 16.0 1.0
CB A:PHE276 4.9 16.5 1.0
N A:ALA274 5.0 16.8 1.0

Reference:

A.G.Pavlovsky, X.Liu, C.R.Faehnle, N.Potente, R.E.Viola. Structural Characterization of Inhibitors with Selectivity Against Members of A Homologous Enzyme Family. Chem.Biol.Drug Des. V. 79 128 2012.
ISSN: ISSN 1747-0277
PubMed: 22039970
DOI: 10.1111/J.1747-0285.2011.01267.X
Page generated: Tue Dec 15 06:22:09 2020

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