Potassium in PDB 5bmo: Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus

The structure of Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus, PDB code: 5bmo was solved by J.Osipiuk, C.Hatzos-Skintges, M.Cuff, M.Endres, G.Babnigg, J.Lohman, M.Ma, J.Rudolf, C.-Y.Chang, B.Shen, A.Joachimiak, Midwest Center Forstructural Genomics (Mcsg), Enzyme Discovery For Natural Productbiosynthesis (Natpro), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 1.92
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.998, 71.998, 284.458, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.5

The binding sites of Potassium atom in the Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus (pdb code 5bmo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus, PDB code: 5bmo:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus within 5.0Å range: probe atom residue distance (Å) B Occ A:K300 b:37.1 occ:1.00 OD1 A:ASP24 2.0 32.2 1.0 NE2 A:HIS135 2.3 29.3 1.0 ND1 A:HIS21 2.4 37.7 1.0 O A:HOH513 2.7 50.2 1.0 CG A:ASP24 2.8 34.5 1.0 OD2 A:ASP24 2.9 32.3 1.0 CE1 A:HIS21 3.1 39.2 1.0 CE1 A:HIS135 3.2 30.9 1.0 CD2 A:HIS135 3.3 27.2 1.0 CG A:HIS21 3.5 36.5 1.0 O A:HOH425 3.5 40.6 1.0 CB A:HIS21 4.0 34.6 1.0 OD1 A:ASP23 4.3 34.2 1.0 CB A:ASP24 4.3 30.2 1.0 NE2 A:HIS21 4.3 38.6 1.0 ND1 A:HIS135 4.3 28.9 1.0 CG A:HIS135 4.4 25.9 1.0 CD2 A:HIS21 4.5 41.1 1.0 N A:HIS21 4.6 26.4 1.0 CA A:ASP24 4.7 31.7 1.0 O A:HIS21 4.8 25.5 1.0 CA A:HIS21 4.8 27.7 1.0 CB A:ALA20 4.8 23.2 1.0 O A:HOH431 4.8 51.5 1.0 N A:ASP24 4.9 30.5 1.0

Potassium binding site 2 out of 3 in the Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus within 5.0Å range: probe atom residue distance (Å) B Occ B:K300 b:36.5 occ:1.00 OD1 B:ASP24 2.1 37.5 1.0 NE2 B:HIS135 2.3 33.8 1.0 ND1 B:HIS21 2.3 35.6 1.0 O B:HOH498 2.5 47.0 1.0 CG B:ASP24 2.8 37.9 1.0 OD2 B:ASP24 2.9 32.9 1.0 CE1 B:HIS135 3.2 35.0 1.0 CE1 B:HIS21 3.2 37.9 1.0 CG B:HIS21 3.3 36.9 1.0 CD2 B:HIS135 3.3 31.9 1.0 CB B:HIS21 3.5 35.8 1.0 O B:HOH416 3.6 45.1 1.0 ND1 B:HIS135 4.3 36.1 1.0 CB B:ASP24 4.3 34.2 1.0 CG B:HIS135 4.4 29.8 1.0 NE2 B:HIS21 4.4 34.8 1.0 OD1 B:ASP23 4.4 51.9 1.0 CD2 B:HIS21 4.4 39.8 1.0 N B:HIS21 4.5 28.6 1.0 CA B:HIS21 4.6 33.1 1.0 CB B:ALA20 4.7 27.8 1.0 CA B:ASP24 4.8 33.1 1.0 O B:HIS21 4.9 30.0 1.0 O B:HOH429 4.9 31.5 1.0 N B:ASP24 5.0 31.3 1.0

Potassium binding site 3 out of 3 in the Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus within 5.0Å range: probe atom residue distance (Å) B Occ C:K300 b:34.5 occ:1.00 OD1 C:ASP24 2.1 39.5 1.0 O C:HOH477 2.3 47.3 1.0 NE2 C:HIS135 2.3 37.0 1.0 ND1 C:HIS21 2.3 34.0 1.0 CG C:ASP24 2.9 35.9 1.0 OD2 C:ASP24 2.9 35.8 1.0 CE1 C:HIS135 3.2 36.4 1.0 CE1 C:HIS21 3.3 39.0 1.0 CD2 C:HIS135 3.3 34.1 1.0 CG C:HIS21 3.3 36.6 1.0 O C:HOH418 3.5 38.6 1.0 CB C:HIS21 3.6 34.3 1.0 CB C:ASP24 4.3 34.5 1.0 OD1 C:ASP23 4.3 55.1 1.0 ND1 C:HIS135 4.3 35.5 1.0 NE2 C:HIS21 4.4 35.9 1.0 CG C:HIS135 4.4 31.2 1.0 CD2 C:HIS21 4.5 37.5 1.0 N C:HIS21 4.6 30.0 1.0 CA C:HIS21 4.7 33.0 1.0 CB C:ALA20 4.8 26.7 1.0 CA C:ASP24 4.8 35.0 1.0 O C:HIS21 4.9 30.6 1.0 N C:ASP24 4.9 35.9 1.0 OD2 C:ASP23 5.0 57.1 1.0 CH3 C:ACT301 5.0 54.8 1.0 O C:HOH437 5.0 29.6 1.0

J.Osipiuk, C.Hatzos-Skintges, M.Cuff, M.Endres, G.Babnigg, J.Lohman, M.Ma, J.Rudolf, C.-Y.Chang, B.Shen, A.Joachimiak, Midwest Center For Structural Genomics (Mcsg), Enzyme Discovery For Natural Product Biosynthesis (Natpro). Lnmx Protein, A Putative Glcnac-Pi De-N-Acetylase From Streptomyces Atroolivaceus. To Be Published.