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Potassium in PDB 1ad4: Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

All present enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus:
2.5.1.15;

Protein crystallography data

The structure of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4 was solved by C.Oefner, D.Kostrewa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 13.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 65.748, 42.142, 99.040, 90.00, 106.06, 90.00
R / Rfree (%) 17.6 / n/a

Other elements in 1ad4:

The structure of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus also contains other interesting chemical elements:

Manganese (Mn) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus (pdb code 1ad4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1ad4

Go back to Potassium Binding Sites List in 1ad4
Potassium binding site 1 out of 2 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K270

b:15.4
occ:1.00
O A:HOH384 2.6 41.5 1.0
O A:VAL75 2.7 13.0 1.0
O A:VAL79 2.8 14.3 1.0
O A:PHE77 2.8 8.5 1.0
O A:HOH383 2.9 23.9 1.0
C A:VAL75 3.7 12.2 1.0
C A:VAL79 3.9 17.5 1.0
C A:PHE77 4.0 11.1 1.0
N A:VAL79 4.2 15.8 1.0
CG1 A:ILE81 4.3 11.3 1.0
CA A:VAL75 4.4 11.4 1.0
N A:PHE77 4.4 12.9 1.0
C A:GLY76 4.4 12.0 1.0
OD2 A:ASP100 4.5 8.5 1.0
CG2 A:VAL75 4.5 14.8 1.0
O A:ILE74 4.7 14.4 1.0
O A:GLY76 4.7 15.1 1.0
N A:GLY76 4.7 14.7 1.0
CA A:LYS80 4.7 16.3 1.0
CA A:PHE77 4.8 9.4 1.0
N A:LYS80 4.8 19.0 1.0
CA A:VAL79 4.8 15.8 1.0
CA A:GLY76 4.8 10.5 1.0
N A:ILE81 5.0 13.1 1.0

Potassium binding site 2 out of 2 in 1ad4

Go back to Potassium Binding Sites List in 1ad4
Potassium binding site 2 out of 2 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K268

b:19.5
occ:1.00
O B:VAL79 2.4 2.0 1.0
O B:PHE77 2.5 10.7 1.0
O B:HOH399 2.6 21.4 1.0
O B:VAL75 3.0 10.6 1.0
C B:VAL79 3.6 6.9 1.0
C B:PHE77 3.7 11.2 1.0
N B:VAL79 3.8 8.4 1.0
C B:VAL75 3.9 12.6 1.0
O B:HOH310 4.1 28.2 1.0
CA B:VAL79 4.4 7.3 1.0
CG1 B:ILE81 4.4 8.2 1.0
N B:PHE77 4.5 14.0 1.0
OD2 B:ASP100 4.5 18.0 1.0
CA B:VAL75 4.5 13.7 1.0
N B:LYS80 4.5 8.1 1.0
N B:ASP78 4.6 11.5 1.0
C B:GLY76 4.6 14.9 1.0
O B:HOH311 4.6 45.6 1.0
CA B:ASP78 4.6 7.7 1.0
CA B:PHE77 4.6 11.5 1.0
CA B:LYS80 4.6 10.4 1.0
C B:ASP78 4.7 7.6 1.0
CG2 B:VAL75 4.8 6.7 1.0
O B:ILE74 4.8 14.2 1.0
N B:GLY76 4.9 14.3 1.0
O B:GLY76 4.9 16.0 1.0
N B:ILE81 4.9 12.9 1.0
CG1 B:VAL79 4.9 4.1 1.0

Reference:

I.C.Hampele, A.D'arcy, G.E.Dale, D.Kostrewa, J.Nielsen, C.Oefner, M.G.Page, H.J.Schonfeld, D.Stuber, R.L.Then. Structure and Function of the Dihydropteroate Synthase From Staphylococcus Aureus. J.Mol.Biol. V. 268 21 1997.
ISSN: ISSN 0022-2836
PubMed: 9149138
DOI: 10.1006/JMBI.1997.0944
Page generated: Sun Dec 13 22:41:26 2020

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