Potassium in PDB 9ccr: Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A

The structure of Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A, PDB code: 9ccr was solved by M.D.Miller, E.D.Hankore, W.Xu, A.J.Kosgei, M.Bhardwaj, J.S.Thorson, S.G.Vanlanen, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.59 / 1.57
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.769, 90.055, 95.718, 90, 90, 90
R / Rfree (%)	17.8 / 20.4

The binding sites of Potassium atom in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A (pdb code 9ccr). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A, PDB code: 9ccr:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A within 5.0Å range: probe atom residue distance (Å) B Occ A:K201 b:41.1 occ:1.00 OE2 A:GLU36 2.3 42.7 0.4 H B:ALA14 2.5 35.2 1.0 HB B:THR12 2.7 36.6 1.0 OH D:TYR23 2.8 38.5 1.0 H B:PHE13 2.9 37.1 1.0 HB2 B:PHE13 3.0 42.0 1.0 CD A:GLU36 3.1 40.2 0.4 HA3 A:GLY32 3.1 39.2 1.0 O A:HOH327 3.1 31.9 1.0 OE1 A:GLU36 3.1 39.8 0.4 HH D:TYR23 3.2 46.3 1.0 N B:ALA14 3.3 29.3 1.0 HB2 B:ALA14 3.3 36.5 1.0 HE1 D:TYR23 3.4 44.4 1.0 N B:PHE13 3.5 30.9 1.0 CZ D:TYR23 3.6 30.3 1.0 C A:GLY32 3.7 32.9 1.0 CB B:THR12 3.7 30.5 1.0 HB3 B:ALA14 3.7 36.5 1.0 CA A:GLY32 3.8 32.6 1.0 N A:ALA33 3.8 30.6 1.0 CB B:PHE13 3.8 34.9 1.0 CE1 D:TYR23 3.8 37.0 1.0 CB B:ALA14 3.8 30.4 1.0 HA41 D:DCC202 3.9 68.9 1.0 H A:ALA33 4.0 36.8 1.0 CA B:PHE13 4.0 31.0 1.0 HA A:ALA33 4.0 40.1 1.0 O A:GLY32 4.0 33.4 1.0 HG1 B:THR12 4.0 37.2 1.0 C B:PHE13 4.1 28.9 1.0 HD2 B:PHE13 4.1 79.1 1.0 CA B:ALA14 4.1 28.7 1.0 OG1 B:THR12 4.2 31.0 1.0 HA2 A:GLY32 4.3 39.2 1.0 C B:THR12 4.3 26.9 1.0 CA B:THR12 4.4 31.3 1.0 HG21 B:THR12 4.4 43.6 1.0 CA A:ALA33 4.5 33.4 1.0 HA B:THR12 4.5 37.6 1.0 CG A:GLU36 4.5 37.6 0.4 CG2 B:THR12 4.5 36.4 1.0 HB3 B:PHE13 4.5 42.0 1.0 HG22 B:THR12 4.5 43.6 1.0 O A:SER29 4.5 26.9 1.0 HA B:ALA14 4.6 34.5 1.0 HG3 A:GLU36 4.6 45.1 0.4 CG B:PHE13 4.6 40.8 1.0 HA62 D:DCC202 4.6 71.7 1.0 CD2 B:PHE13 4.6 65.9 1.0 HB2 A:ALA33 4.6 38.2 1.0 HB2 A:GLU36 4.7 49.0 0.6 CE2 D:TYR23 4.7 28.1 1.0 HB1 B:ALA14 4.8 36.5 1.0 CA4 D:DCC202 4.8 57.4 1.0 O B:HOH378 4.8 39.2 1.0 H A:GLY32 4.9 36.4 1.0 N A:GLY32 4.9 30.3 1.0 HA B:PHE13 4.9 37.2 1.0 HE2 D:TYR23 5.0 33.8 1.0 HG2 A:GLU36 5.0 45.1 0.4

Potassium binding site 2 out of 4 in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A within 5.0Å range: probe atom residue distance (Å) B Occ B:K201 b:40.2 occ:1.00 OE2 B:GLU36 2.4 37.2 0.4 OE1 B:GLU36 2.5 31.7 0.4 H A:ALA14 2.6 31.5 1.0 HB A:THR12 2.7 32.2 1.0 CD B:GLU36 2.8 31.8 0.4 OH C:TYR23 2.8 43.3 1.0 H A:PHE13 2.9 31.6 1.0 HB2 A:PHE13 3.0 36.5 1.0 O B:HOH329 3.0 32.2 1.0 HH C:TYR23 3.0 52.0 1.0 HA3 B:GLY32 3.1 33.8 1.0 N A:ALA14 3.3 26.2 1.0 HB2 A:ALA14 3.4 29.8 1.0 N A:PHE13 3.4 26.3 1.0 HE1 C:TYR23 3.5 46.4 1.0 C B:GLY32 3.5 28.2 1.0 CZ C:TYR23 3.7 33.5 1.0 CB A:THR12 3.7 26.8 1.0 N B:ALA33 3.7 25.7 1.0 HA B:ALA33 3.8 35.1 1.0 CA B:GLY32 3.8 28.2 1.0 CB A:PHE13 3.8 30.4 1.0 HB3 A:ALA14 3.8 29.8 1.0 HG1 A:THR12 3.8 37.7 1.0 O B:GLY32 3.8 27.5 1.0 CE1 C:TYR23 3.9 38.6 1.0 H B:ALA33 3.9 30.9 1.0 CB A:ALA14 3.9 24.8 1.0 CA A:PHE13 3.9 26.2 1.0 C A:PHE13 4.1 23.2 1.0 HA41 C:DCC202 4.1 60.0 1.0 CA A:ALA14 4.2 21.9 1.0 HD2 A:PHE13 4.2 61.0 1.0 HA2 B:GLY32 4.2 33.8 1.0 CA B:ALA33 4.2 29.2 1.0 OG1 A:THR12 4.3 31.4 1.0 CG B:GLU36 4.3 32.5 0.4 HB2 B:GLU36 4.3 37.9 0.6 C A:THR12 4.3 27.0 1.0 HG21 A:THR12 4.4 41.4 1.0 HB2 B:ALA33 4.4 31.8 1.0 CA A:THR12 4.5 27.5 1.0 HB3 A:PHE13 4.5 36.5 1.0 HA A:THR12 4.5 33.0 1.0 CG A:PHE13 4.5 33.2 1.0 CG2 A:THR12 4.5 34.5 1.0 HA A:ALA14 4.5 26.3 1.0 O B:SER29 4.6 26.0 1.0 HG3 B:GLU36 4.6 39.1 0.4 HB2 B:GLU36 4.6 37.9 0.4 CD2 A:PHE13 4.6 50.8 1.0 HG22 A:THR12 4.6 41.4 1.0 HG2 B:GLU36 4.7 39.1 0.4 CE2 C:TYR23 4.8 33.4 1.0 HB1 A:ALA14 4.8 29.8 1.0 HA A:PHE13 4.9 31.4 1.0 N B:GLY32 4.9 25.6 1.0 CB B:ALA33 4.9 26.5 1.0 H B:GLY32 4.9 30.8 1.0 O A:HOH354 5.0 37.6 1.0 HB3 B:GLU36 5.0 37.9 0.6 HE1 C:PHE24 5.0 28.3 1.0

Potassium binding site 3 out of 4 in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A within 5.0Å range: probe atom residue distance (Å) B Occ C:K201 b:44.9 occ:1.00 H D:ALA14 2.4 30.3 1.0 OE2 C:GLU36 2.6 38.3 0.7 HB D:THR12 2.7 34.1 1.0 OH B:TYR23 2.8 38.7 1.0 OE1 C:GLU36 2.9 46.7 0.7 H D:PHE13 3.0 34.0 1.0 HB2 D:PHE13 3.0 35.7 1.0 CD C:GLU36 3.1 34.6 0.7 O C:HOH344 3.1 34.8 1.0 HB2 D:ALA14 3.1 32.5 1.0 HA3 C:GLY32 3.2 39.4 1.0 N D:ALA14 3.2 25.2 1.0 HH B:TYR23 3.2 46.5 1.0 HE1 B:TYR23 3.4 39.5 1.0 N D:PHE13 3.5 28.3 1.0 HB3 D:ALA14 3.6 32.5 1.0 CB D:THR12 3.6 28.4 1.0 CZ B:TYR23 3.7 29.4 1.0 C C:GLY32 3.7 34.4 1.0 CB D:ALA14 3.7 27.0 1.0 N C:ALA33 3.8 27.2 1.0 CE1 B:TYR23 3.8 32.9 1.0 CA C:GLY32 3.9 32.8 1.0 CB D:PHE13 3.9 29.7 1.0 HG1 D:THR12 3.9 40.3 1.0 HA C:ALA33 3.9 36.5 1.0 CA D:PHE13 4.0 28.8 1.0 H C:ALA33 4.0 32.6 1.0 C D:PHE13 4.0 26.3 1.0 CA D:ALA14 4.0 24.6 1.0 O C:GLY32 4.0 35.9 1.0 OG1 D:THR12 4.1 33.6 1.0 HA41 B:DCC202 4.2 64.2 1.0 C D:THR12 4.3 28.1 1.0 HG21 D:THR12 4.3 39.7 1.0 CA C:ALA33 4.4 30.4 1.0 HA2 C:GLY32 4.4 39.4 1.0 HA D:ALA14 4.4 29.5 1.0 CA D:THR12 4.5 27.4 1.0 HB3 D:PHE13 4.5 35.7 1.0 HB2 C:GLU36 4.5 41.8 0.3 HB2 C:ALA33 4.5 39.1 1.0 CG2 D:THR12 4.5 33.1 1.0 O C:SER29 4.5 26.0 1.0 CG C:GLU36 4.6 34.1 0.7 HA D:THR12 4.6 32.9 1.0 HB1 D:ALA14 4.6 32.5 1.0 HG22 D:THR12 4.7 39.7 1.0 CE2 B:TYR23 4.8 27.7 1.0 CG D:PHE13 4.8 31.7 1.0 HG3 C:GLU36 4.8 40.9 0.7 O D:HOH395 4.9 41.3 1.0 H C:GLY32 4.9 34.5 1.0 HB2 C:GLU36 4.9 41.8 0.7 N C:GLY32 4.9 28.7 1.0 HA D:PHE13 4.9 34.6 1.0 H D:ASP15 5.0 32.3 1.0 HE2 B:TYR23 5.0 33.3 1.0

Potassium binding site 4 out of 4 in the Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of the ESPE7 Thioesterase Mutant R35A From the Esperamicin Biosynthetic Pathway at 1.6 A within 5.0Å range: probe atom residue distance (Å) B Occ D:K201 b:39.8 occ:1.00 OE1 D:GLU36 2.4 34.6 0.6 OE2 D:GLU36 2.5 36.6 0.6 H C:ALA14 2.5 33.9 1.0 HB C:THR12 2.7 34.8 1.0 CD D:GLU36 2.7 35.8 0.6 OH A:TYR23 2.9 36.6 1.0 HB2 C:PHE13 3.0 36.4 1.0 H C:PHE13 3.0 34.8 1.0 HA3 D:GLY32 3.1 32.9 1.0 O D:HOH328 3.1 31.4 1.0 N C:ALA14 3.3 28.2 1.0 HB2 C:ALA14 3.3 35.3 1.0 HH A:TYR23 3.3 44.0 1.0 HE1 A:TYR23 3.4 34.8 1.0 N C:PHE13 3.5 28.9 1.0 C D:GLY32 3.6 28.7 1.0 CB C:THR12 3.7 29.0 1.0 CZ A:TYR23 3.7 27.6 1.0 N D:ALA33 3.8 25.5 1.0 CA D:GLY32 3.8 27.4 1.0 CB C:PHE13 3.8 30.3 1.0 HA D:ALA33 3.8 29.5 1.0 CE1 A:TYR23 3.9 29.0 1.0 HB3 C:ALA14 3.9 35.3 1.0 CB C:ALA14 3.9 29.4 1.0 H D:ALA33 3.9 30.6 1.0 O D:GLY32 4.0 30.1 1.0 CA C:PHE13 4.0 26.9 1.0 C C:PHE13 4.1 26.5 1.0 HG1 C:THR12 4.1 41.3 1.0 HA41 A:DCC202 4.1 60.1 1.0 CA C:ALA14 4.1 22.4 1.0 CG D:GLU36 4.2 33.3 0.6 OG1 C:THR12 4.2 34.4 1.0 HA2 D:GLY32 4.3 32.9 1.0 C C:THR12 4.3 27.1 1.0 CA D:ALA33 4.3 24.5 1.0 HG21 C:THR12 4.4 42.0 1.0 HB2 D:GLU36 4.4 38.1 0.4 CA C:THR12 4.5 32.6 1.0 HG3 D:GLU36 4.5 39.9 0.6 HB3 C:PHE13 4.5 36.4 1.0 HA C:ALA14 4.5 26.9 1.0 CG2 C:THR12 4.5 35.0 1.0 HA C:THR12 4.5 39.2 1.0 CG C:PHE13 4.5 36.8 1.0 HB2 D:ALA33 4.5 31.1 1.0 HD2 C:PHE13 4.5 63.8 1.0 HB2 D:GLU36 4.6 38.8 0.6 O D:SER29 4.6 25.6 1.0 HG22 C:THR12 4.6 42.0 1.0 HG2 D:GLU36 4.8 39.9 0.6 HB1 C:ALA14 4.8 35.3 1.0 CD2 C:PHE13 4.8 53.1 1.0 CE2 A:TYR23 4.9 31.4 1.0 H D:GLY32 4.9 32.7 1.0 N D:GLY32 4.9 27.2 1.0 HA C:PHE13 4.9 32.3 1.0 CB D:GLU36 5.0 32.3 0.6

E.D.Hankore, M.D.Miller, A.J.Kosgei, W.Xu, K.Tan, M.Endres, M.Bhardwaj, G.Joachimiak, A.Joachimiak, G.N.Phillips Jr., J.S.Thorson, S.G.Van Lanen. Functional and Structural Studies on the Esperamicin Thioesterase and Progress Toward Understanding Enediyne Core Biosynthesis To Be Published.