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Sodium in PDB 3moe: The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp

Enzymatic activity of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp

All present enzymatic activity of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp:
4.1.1.32;

Protein crystallography data

The structure of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp, PDB code: 3moe was solved by T.A.Johnson, T.Holyoak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.57 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.324, 119.117, 60.053, 90.00, 111.19, 90.00
R / Rfree (%) 14.8 / 17.4

Other elements in 3moe:

The structure of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp (pdb code 3moe). 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 The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp, PDB code: 3moe:

Sodium binding site 1 out of 1 in 3moe

Go back to Sodium Binding Sites List in 3moe
Sodium binding site 1 out of 1 in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na800

b:22.8
occ:0.80
O A:ASN208 2.0 13.1 1.0
O A:HOH772 2.2 14.0 1.0
O A:LEU79 2.2 8.0 1.0
O A:HOH787 2.4 12.9 1.0
O A:HOH769 2.5 24.7 1.0
C A:ASN208 3.1 13.3 1.0
C A:LEU79 3.3 6.3 1.0
CB A:ASN208 3.6 19.3 1.0
N A:LEU79 3.7 4.1 1.0
CA A:LEU79 3.8 5.6 1.0
CB A:LEU79 3.8 5.4 1.0
CA A:ASN208 3.9 15.9 1.0
CB A:ASN209 4.0 16.2 1.0
N A:ASN209 4.1 13.8 1.0
O A:VAL65 4.1 10.9 1.0
C A:ASN209 4.2 9.4 1.0
O A:ASN209 4.2 11.1 1.0
CA A:ASN209 4.3 14.4 1.0
O A:HOH1087 4.4 28.3 1.0
O A:GLY64 4.4 16.8 1.0
N A:TRP210 4.5 8.8 1.0
CB A:TRP210 4.5 5.8 1.0
N A:THR80 4.5 5.2 1.0
CA A:THR80 4.9 3.5 1.0
C A:ALA78 4.9 3.2 1.0
C A:VAL65 4.9 10.8 1.0
CA A:TRP210 4.9 6.5 1.0
CG A:LEU79 5.0 5.5 1.0
CG A:ASN208 5.0 25.0 1.0

Reference:

T.A.Johnson, T.Holyoak. Increasing the Conformational Entropy of the Omega-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity . Biochemistry V. 49 5176 2010.
ISSN: ISSN 0006-2960
PubMed: 20476774
DOI: 10.1021/BI100399E
Page generated: Tue Dec 15 06:17:54 2020

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