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Potassium in PDB 1wxx: Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8

Protein crystallography data

The structure of Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8, PDB code: 1wxx was solved by A.A.Pioszak, K.Murayama, N.Nakagawa, A.Ebihara, S.Kuramitsu, M.Shirouzu, S.Yokoyama, Riken Structural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.55 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 77.551, 82.318, 79.616, 96.34, 90.14, 103.06
R / Rfree (%) 20.3 / 22.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8 (pdb code 1wxx). 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 TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8, PDB code: 1wxx:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 1wxx

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Potassium binding site 1 out of 4 in the Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8


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 TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1400

b:20.4
occ:1.00
 O A:HOH1788 2.6 33.2 1.0
O A:GLN190 2.6 26.6 1.0
O A:ASP185 2.7 19.0 1.0
O A:ARG187 2.8 26.1 1.0
O A:HOH1667 2.9 28.4 1.0
OG1 A:THR192 3.0 17.8 1.0
N A:THR192 3.6 20.1 1.0
C A:GLN190 3.8 28.4 1.0
CA A:THR192 3.8 17.2 1.0
C A:ARG187 3.8 26.0 1.0
C A:ASP185 3.8 20.2 1.0
C A:LEU186 3.9 21.9 1.0
O A:HOH1589 3.9 23.1 1.0
CB A:THR192 4.0 17.2 1.0
N A:ARG187 4.1 23.2 1.0
C A:LYS191 4.1 22.9 1.0
CA A:LEU186 4.1 20.5 1.0
O A:LEU186 4.1 20.9 1.0
O A:ALA188 4.3 32.2 1.0
N A:LEU186 4.4 20.2 1.0
CE A:LYS147 4.4 26.4 1.0
O A:LYS191 4.6 21.0 1.0
CA A:ARG187 4.6 25.1 1.0
N A:GLN190 4.6 31.2 1.0
CA A:GLN190 4.6 29.7 1.0
N A:LYS191 4.6 26.2 1.0
N A:ALA188 4.7 27.6 1.0
CA A:LYS191 4.7 25.9 1.0
C A:ALA188 4.7 31.3 1.0
CA A:ALA188 4.8 29.9 1.0
CG2 A:THR192 4.8 16.0 1.0
CB A:GLN190 4.9 30.4 1.0
CB A:ASP185 5.0 22.4 1.0
CA A:ASP185 5.0 20.0 1.0

Potassium binding site 2 out of 4 in 1wxx

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Potassium binding site 2 out of 4 in the Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8


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 TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1401

b:24.1
occ:1.00
 O B:ASP185 2.6 19.2 1.0
O B:HOH1798 2.7 34.8 1.0
O B:HOH1778 2.8 36.2 1.0
O B:GLN190 2.8 29.7 1.0
OG1 B:THR192 3.0 19.9 1.0
O B:ARG187 3.0 25.8 1.0
N B:THR192 3.5 22.0 1.0
CA B:THR192 3.7 19.9 1.0
C B:ASP185 3.7 19.2 1.0
C B:GLN190 3.8 31.5 1.0
CB B:THR192 3.9 19.8 1.0
C B:ARG187 3.9 26.8 1.0
C B:LEU186 3.9 21.9 1.0
O B:HOH1562 4.0 21.6 1.0
C B:LYS191 4.0 25.5 1.0
N B:ARG187 4.0 23.1 1.0
CA B:LEU186 4.1 20.0 1.0
O B:LEU186 4.3 23.2 1.0
N B:LEU186 4.4 19.0 1.0
CE B:LYS147 4.4 25.9 1.0
CA B:LYS191 4.6 28.7 1.0
O B:LYS191 4.6 23.6 1.0
N B:LYS191 4.6 29.9 1.0
CA B:ARG187 4.6 25.7 1.0
N B:GLN190 4.7 34.2 1.0
CG2 B:THR192 4.7 18.7 1.0
CA B:GLN190 4.7 32.8 1.0
CB B:ASP185 4.8 21.8 1.0
N B:ALA188 4.8 28.7 1.0
CA B:ASP185 4.8 19.8 1.0
CB B:GLN190 4.9 34.0 1.0
OD1 B:ASP185 4.9 25.2 1.0

Potassium binding site 3 out of 4 in 1wxx

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Potassium binding site 3 out of 4 in the Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8


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 TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1402

b:19.5
occ:1.00
 O C:GLN190 2.7 24.0 1.0
O C:ASP185 2.8 17.1 1.0
O C:ARG187 2.9 18.9 1.0
O C:HOH1552 2.9 22.3 1.0
OG1 C:THR192 3.0 17.4 1.0
N C:THR192 3.6 17.0 1.0
C C:GLN190 3.7 26.0 1.0
CA C:THR192 3.8 15.1 1.0
C C:ASP185 3.8 18.1 1.0
C C:ARG187 3.9 20.8 1.0
C C:LEU186 3.9 18.7 1.0
CB C:THR192 4.0 15.7 1.0
C C:LYS191 4.0 19.8 1.0
O C:HOH1605 4.0 17.6 1.0
N C:ARG187 4.1 19.7 1.0
CA C:LEU186 4.1 19.2 1.0
O C:LEU186 4.2 18.3 1.0
N C:LEU186 4.4 18.1 1.0
O C:LYS191 4.5 16.8 1.0
N C:GLN190 4.6 28.4 1.0
N C:LYS191 4.6 23.9 1.0
CA C:GLN190 4.6 27.3 1.0
CA C:LYS191 4.6 23.3 1.0
CA C:ARG187 4.7 20.7 1.0
N C:ALA188 4.8 21.1 1.0
O C:HOH1730 4.8 32.8 1.0
CB C:GLN190 4.8 28.5 1.0
CG2 C:THR192 4.9 16.4 1.0
CA C:ALA188 4.9 23.1 1.0
O C:ALA188 4.9 25.3 1.0
CB C:ASP185 4.9 21.1 1.0
C C:ALA188 4.9 24.4 1.0
CA C:ASP185 5.0 19.1 1.0

Potassium binding site 4 out of 4 in 1wxx

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Potassium binding site 4 out of 4 in the Crystal Structure of TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8


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 TT1595, A Putative Sam-Dependent Methyltransferase From Thermus Thermophillus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1403

b:25.0
occ:1.00
 O D:GLN190 2.6 31.3 1.0
O D:ASP185 2.7 23.2 1.0
O D:HOH1483 2.7 24.1 1.0
O D:ARG187 2.8 31.0 1.0
O D:HOH1575 2.8 35.9 1.0
OG1 D:THR192 3.1 20.3 1.0
N D:THR192 3.6 23.5 1.0
C D:GLN190 3.7 32.5 1.0
C D:ARG187 3.7 31.4 1.0
CA D:THR192 3.8 21.1 1.0
C D:ASP185 3.8 23.7 1.0
C D:LEU186 3.9 25.1 1.0
O D:HOH1547 4.0 31.7 1.0
N D:ARG187 4.0 27.2 1.0
CB D:THR192 4.0 21.1 1.0
C D:LYS191 4.0 26.5 1.0
CA D:LEU186 4.2 24.0 1.0
O D:LEU186 4.2 24.9 1.0
NZ D:LYS147 4.4 34.5 1.0
N D:LEU186 4.4 23.0 1.0
O D:ALA188 4.5 37.8 1.0
N D:GLN190 4.5 35.5 1.0
CA D:ARG187 4.5 29.6 1.0
CA D:GLN190 4.5 33.9 1.0
N D:LYS191 4.5 30.6 1.0
O D:LYS191 4.5 26.0 1.0
CA D:LYS191 4.6 29.6 1.0
N D:ALA188 4.6 33.2 1.0
C D:ALA188 4.7 36.9 1.0
CB D:GLN190 4.7 34.9 1.0
CA D:ALA188 4.8 35.5 1.0
CG2 D:THR192 4.9 20.4 1.0
CB D:ASP185 4.9 25.1 1.0
CA D:ASP185 5.0 23.8 1.0

Reference:

A.A.Pioszak, K.Murayama, N.Nakagawa, A.Ebihara, S.Kuramitsu, M.Shirouzu, S.Yokoyama. Structures of A Putative Rna 5-Methyluridine Methyltransferase, Thermus Thermophilus TTHA1280, and Its Complex with S-Adenosyl-L-Homocysteine. Acta Crystallogr.,Sect.F V. 61 867 2005.
ISSN: ESSN 1744-3091
PubMed: 16511182
DOI: 10.1107/S1744309105029842
Page generated: Mon Aug 12 05:44:17 2024

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