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Sodium in PDB 3qvw: L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A

Enzymatic activity of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A

All present enzymatic activity of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A:
5.5.1.4;

Protein crystallography data

The structure of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A, PDB code: 3qvw was solved by K.Neelon, M.F.Roberts, B.Stec, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.20 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.260, 89.940, 104.865, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 28.2

Sodium Binding Sites:

The binding sites of Sodium atom in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A (pdb code 3qvw). 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 L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A, PDB code: 3qvw:

Sodium binding site 1 out of 1 in 3qvw

Go back to Sodium Binding Sites List in 3qvw
Sodium binding site 1 out of 1 in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Fulgidus Mutant K278A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na525

b:36.3
occ:0.50
OD2 A:ASP329 2.5 14.3 1.0
O A:HOH610 3.5 35.0 0.5
CG A:ASP329 3.5 14.2 1.0
CB A:ASP329 4.1 13.7 1.0
OD1 A:ASP329 4.5 14.3 1.0

Reference:

K.Neelon, M.F.Roberts, B.Stec. Atomic Crowding Drives the Catalysis of Myo-Inositol Phosphate Synthase, As Deduced From A Crystal Structure of A Trapped Catalytic Intermediate To Be Published.
Page generated: Tue Dec 15 06:23:14 2020

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