Potassium in PDB 3qw2: L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A

All present enzymatic activity of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A:
5.5.1.4;

The structure of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A, PDB code: 3qw2 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)	103.14 / 2.59
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	91.512, 88.036, 103.727, 90.00, 94.91, 90.00
R / Rfree (%)	18.5 / 26.7

The binding sites of Potassium atom in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A (pdb code 3qw2). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A, PDB code: 3qw2:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A within 5.0Å range: probe atom residue distance (Å) B Occ A:K394 b:45.3 occ:1.00 OH C:TYR325 2.6 10.4 1.0 OD2 D:ASP329 2.7 13.2 1.0 OD2 A:ASP329 2.9 14.0 1.0 OH B:TYR325 3.3 11.3 1.0 CZ C:TYR325 3.6 10.1 1.0 CG D:ASP329 3.7 13.0 1.0 CE1 B:TYR325 3.8 11.3 1.0 CE1 C:TYR325 3.8 9.9 1.0 CG A:ASP329 3.8 14.9 1.0 CD C:LYS323 3.9 11.4 1.0 CD B:LYS323 3.9 11.7 1.0 O A:HOH477 3.9 12.9 1.0 CZ B:TYR325 3.9 11.2 1.0 O A:HOH452 4.0 2.0 1.0 O D:HOH486 4.1 7.6 1.0 CB A:ASP329 4.1 14.1 1.0 CB D:ASP329 4.2 12.2 1.0 NZ C:LYS323 4.3 11.8 1.0 NZ B:LYS323 4.3 14.3 1.0 O B:HOH408 4.4 2.0 1.0 CB C:LYS323 4.5 10.9 1.0 CE C:LYS323 4.7 11.8 1.0 OD1 D:ASP329 4.8 16.4 1.0 CE B:LYS323 4.8 11.9 1.0 OD1 A:ASP329 4.8 19.4 1.0 CB B:LYS323 4.9 11.5 1.0 CG C:LYS323 4.9 11.3 1.0 CE2 C:TYR325 4.9 11.2 1.0 CD1 B:TYR325 5.0 11.0 1.0

Potassium binding site 2 out of 3 in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A within 5.0Å range: probe atom residue distance (Å) B Occ C:K398 b:90.2 occ:1.00 O1N C:NAD396 2.3 45.0 1.0 OD2 C:ASP304 2.9 20.1 1.0 O7N C:NAD396 3.1 52.5 1.0 O C:HOH427 3.5 22.2 1.0 PN C:NAD396 3.7 43.7 1.0 OD2 C:ASP332 3.8 26.8 1.0 CB C:ASP332 4.0 16.1 1.0 O5D C:NAD396 4.0 45.0 1.0 O3 C:NAD396 4.1 41.8 1.0 CG C:ASP304 4.1 18.7 1.0 C7N C:NAD396 4.2 52.1 1.0 CG2 C:ILE11 4.2 12.5 1.0 CG C:ASP332 4.4 20.1 1.0 OD1 C:ASP304 4.5 18.6 1.0 OD1 C:ASP261 4.6 57.4 1.0 CB C:ASP261 4.6 57.2 1.0 CG2 C:VAL12 4.6 13.1 1.0 O C:HOH447 4.7 8.1 1.0 N C:ALA333 4.9 14.5 1.0 N7N C:NAD396 4.9 53.4 1.0 O2N C:NAD396 4.9 41.4 1.0 C2N C:NAD396 4.9 52.9 1.0 CD1 C:LEU257 5.0 25.1 1.0 O C:HOH522 5.0 12.4 1.0

Potassium binding site 3 out of 3 in the L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of L-Myo-Inositol 1-Phosphate Synthase From Archaeoglobus Mutant N255A within 5.0Å range: probe atom residue distance (Å) B Occ D:K397 b:88.3 occ:1.00 O1N D:NAD396 2.5 40.6 1.0 O7N D:NAD396 2.6 36.2 1.0 OD2 D:ASP304 2.9 20.2 1.0 O D:HOH453 3.3 21.1 1.0 OD1 D:ASP304 3.4 19.8 1.0 CG D:ASP304 3.5 19.9 1.0 CB D:ASP332 3.5 15.4 1.0 CG2 D:ILE11 3.6 12.4 1.0 PN D:NAD396 3.9 42.0 1.0 CG2 D:VAL12 3.9 12.7 1.0 N D:ALA333 4.0 12.8 1.0 C7N D:NAD396 4.0 39.0 1.0 C D:ASP332 4.2 13.5 1.0 OD2 D:ASP332 4.2 27.1 1.0 CA D:ALA333 4.4 12.4 1.0 CG D:ASP332 4.4 20.2 1.0 CA D:ASP332 4.5 14.5 1.0 O2N D:NAD396 4.5 39.4 1.0 O3 D:NAD396 4.5 36.2 1.0 CB D:ALA333 4.6 12.4 1.0 N7N D:NAD396 4.7 39.0 1.0 O D:ASP332 4.8 13.3 1.0 O D:HOH484 4.9 30.8 1.0 C2N D:NAD396 4.9 41.1 1.0 C3N D:NAD396 5.0 39.4 1.0 CB D:ASP304 5.0 19.2 1.0 N D:VAL12 5.0 14.0 1.0

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.