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Potassium in PDB 1ta9: Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe

Enzymatic activity of Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe

All present enzymatic activity of Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe:
1.1.1.6;

Protein crystallography data

The structure of Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe, PDB code: 1ta9 was solved by A.M.Mulichak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 105.980, 105.980, 140.630, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 20.9

Other elements in 1ta9:

The structure of Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe (pdb code 1ta9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe, PDB code: 1ta9:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1ta9

Go back to Potassium Binding Sites List in 1ta9
Potassium binding site 1 out of 2 in the Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe


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 Glycerol Dehydrogenase From Schizosaccharomyces Pombe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1503

b:17.6
occ:1.00
O A:HOH1540 2.6 12.2 1.0
OD2 A:ASP182 2.6 22.1 1.0
O A:ASP232 2.7 12.7 1.0
OG1 A:THR236 2.9 13.3 1.0
OG A:SER235 3.0 12.8 1.0
OD2 A:ASP232 3.2 14.4 1.0
O3 A:GOL1401 3.3 30.9 1.0
OG A:SER302 3.7 13.7 1.0
CE1 A:HIS315 3.7 16.1 1.0
C A:ASP232 3.7 12.2 1.0
CG A:ASP182 3.7 22.0 1.0
N A:THR236 3.8 12.2 1.0
CG A:ASP232 3.9 13.9 1.0
CA A:THR236 4.1 12.4 1.0
CB A:THR236 4.1 12.4 1.0
NE2 A:HIS315 4.1 16.2 1.0
OD1 A:ASP182 4.2 21.8 1.0
ZN A:ZN1502 4.2 33.9 1.0
CB A:SER235 4.3 12.4 1.0
OD1 A:ASP232 4.4 14.3 1.0
CB A:PHE306 4.4 15.7 1.0
C A:SER235 4.5 12.2 1.0
CA A:ASP232 4.5 12.5 1.0
C3 A:GOL1401 4.5 31.1 1.0
N A:ALA233 4.6 11.9 1.0
CB A:ASP232 4.6 12.9 1.0
CA A:ALA233 4.7 11.8 1.0
ND1 A:HIS315 4.7 16.0 1.0
OE2 A:GLU239 4.7 14.9 1.0
CA A:SER235 4.8 12.1 1.0
O A:HOH1511 4.9 9.2 1.0
CG A:PHE306 4.9 16.3 1.0
N A:SER235 4.9 12.2 1.0
CD2 A:PHE306 5.0 16.5 1.0
CG2 A:THR236 5.0 12.5 1.0

Potassium binding site 2 out of 2 in 1ta9

Go back to Potassium Binding Sites List in 1ta9
Potassium binding site 2 out of 2 in the Crystal Structure of Glycerol Dehydrogenase From Schizosaccharomyces Pombe


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 Glycerol Dehydrogenase From Schizosaccharomyces Pombe within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1504

b:17.2
occ:1.00
O B:HOH1526 2.6 15.0 1.0
OD2 B:ASP182 2.7 20.1 1.0
O B:ASP232 2.8 12.3 1.0
OG1 B:THR236 3.0 12.9 1.0
OG B:SER235 3.2 13.9 1.0
O3 B:GOL1402 3.2 31.5 1.0
OD2 B:ASP232 3.3 13.8 1.0
CE1 B:HIS315 3.6 15.9 1.0
OG B:SER302 3.7 12.5 1.0
CG B:ASP182 3.7 19.6 1.0
C B:ASP232 3.7 12.0 1.0
CG B:ASP232 3.9 13.4 1.0
N B:THR236 3.9 12.1 1.0
OD1 B:ASP182 4.1 19.2 1.0
CA B:THR236 4.1 12.0 1.0
NE2 B:HIS315 4.1 16.0 1.0
CB B:THR236 4.2 12.2 1.0
ZN B:ZN1501 4.2 34.2 1.0
OD1 B:ASP232 4.3 13.4 1.0
C3 B:GOL1402 4.4 31.8 1.0
CB B:PHE306 4.5 15.4 1.0
CA B:ASP232 4.5 12.0 1.0
C B:SER235 4.5 12.2 1.0
CB B:SER235 4.5 12.6 1.0
ND1 B:HIS315 4.6 15.6 1.0
N B:ALA233 4.6 11.7 1.0
CB B:ASP232 4.6 12.4 1.0
OE2 B:GLU239 4.7 15.4 1.0
CA B:ALA233 4.7 11.9 1.0
O B:HOH1520 4.9 10.8 1.0
CG B:PHE306 4.9 16.2 1.0
CA B:SER235 4.9 12.3 1.0
CD2 B:PHE306 5.0 16.5 1.0
N B:SER235 5.0 12.3 1.0
CD2 B:LEU311 5.0 14.3 1.0

Reference:

A.M.Mulichak, A.M.Mulichak. N/A N/A.
Page generated: Mon Aug 12 05:28:43 2024

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