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Sodium in PDB 1ygg: Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes

Enzymatic activity of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes

All present enzymatic activity of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes:
4.1.1.49;

Protein crystallography data

The structure of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes, PDB code: 1ygg was solved by Y.A.Leduc, L.Prasad, M.Laivenieks, J.G.Zeikus, L.T.Delbaere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.36 / 1.85
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 102.090, 102.090, 72.120, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 20.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes (pdb code 1ygg). 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 Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes, PDB code: 1ygg:

Sodium binding site 1 out of 1 in 1ygg

Go back to Sodium Binding Sites List in 1ygg
Sodium binding site 1 out of 1 in the Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobacillus Succinogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1000

b:35.8
occ:1.00
OD1 A:ASP307 2.7 30.2 1.0
O A:TYR29 2.8 28.9 1.0
O A:HOH675 2.9 33.8 1.0
C A:TYR29 3.6 30.7 1.0
CD1 A:TYR29 3.7 30.6 1.0
CA A:ASP307 3.7 28.1 1.0
CG A:ASP307 3.8 32.0 1.0
CB A:TYR29 3.8 30.1 1.0
CE1 A:HIS146 3.9 29.8 1.0
CA A:TYR29 3.9 30.2 1.0
CB A:PHE33 3.9 30.1 1.0
N A:PHE33 3.9 28.8 1.0
N A:ASP307 4.1 25.5 1.0
NE2 A:HIS146 4.2 30.1 1.0
CG A:TYR29 4.2 30.2 1.0
CA A:PHE33 4.2 31.2 1.0
CB A:ASP307 4.3 28.4 1.0
O A:HOH618 4.3 27.2 1.0
CB A:LEU32 4.4 30.5 1.0
ND1 A:HIS146 4.5 29.6 1.0
CD A:ARG306 4.6 30.7 1.0
O A:HOH734 4.7 34.0 1.0
C A:LEU32 4.7 29.7 1.0
N A:GLU30 4.7 32.1 1.0
CE1 A:TYR29 4.8 30.2 1.0
C A:ASP307 4.8 27.5 1.0
CG A:ARG306 4.8 28.4 1.0
OD2 A:ASP307 4.8 30.9 1.0
OE1 A:GLU36 4.9 30.7 1.0
CD2 A:HIS146 5.0 26.6 1.0
O A:ASP307 5.0 27.7 1.0

Reference:

Y.A.Leduc, L.Prasad, M.Laivenieks, J.G.Zeikus, L.T.Delbaere. Structure of Pep Carboxykinase From the Succinate-Producing Actinobacillus Succinogenes: A New Conserved Active-Site Motif. Acta Crystallogr.,Sect.D V. 61 903 2005.
ISSN: ISSN 0907-4449
PubMed: 15983413
DOI: 10.1107/S0907444905008723
Page generated: Tue Dec 15 05:42:18 2020

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