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Potassium in PDB 8cfe: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03

Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03:
3.3.1.1;

Protein crystallography data

The structure of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03, PDB code: 8cfe was solved by P.H.Malecki, M.Gawel, M.Stepniewska, K.Brzezinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.72 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 175.13, 104.08, 107.9, 90, 100.65, 90
R / Rfree (%) 15.7 / 20.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03 (pdb code 8cfe). 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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03, PDB code: 8cfe:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 8cfe

Go back to Potassium Binding Sites List in 8cfe
Potassium binding site 1 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:27.6
occ:1.00
O A:THR380 2.7 23.7 1.0
O A:HIS382 2.8 26.1 1.0
O A:HOH680 2.8 25.4 1.0
OG1 A:THR380 2.8 25.0 1.0
O A:HOH841 2.8 26.7 1.0
O B:HOH754 2.9 28.1 1.0
OE1 A:GLN65 3.3 25.5 1.0
NE2 A:GLN65 3.5 25.2 1.0
CD A:GLN65 3.5 26.4 1.0
CB A:THR380 3.5 26.2 1.0
C A:THR380 3.6 23.4 1.0
C A:HIS382 3.6 22.8 1.0
O A:GLY381 3.7 27.1 1.0
CA A:PRO383 4.0 25.7 1.0
C A:GLY381 4.1 25.8 1.0
N6 A:ADE502 4.1 25.6 1.0
N A:PRO383 4.2 25.8 1.0
CA A:THR380 4.2 25.5 1.0
CB B:ASP216 4.3 23.3 1.0
N A:HIS382 4.5 24.1 1.0
N A:GLY381 4.5 25.2 1.0
CG B:ASP216 4.5 28.9 1.0
OD1 B:ASP216 4.6 31.7 1.0
CA A:HIS382 4.7 24.3 1.0
CG A:GLN65 4.7 25.4 1.0
O A:HOH950 4.7 29.3 1.0
C A:PRO383 4.7 27.1 1.0
CA A:GLY381 4.7 23.0 1.0
N A:SER384 4.8 24.5 1.0
CG2 A:THR380 4.9 29.4 1.0
O B:ASP216 4.9 27.4 1.0
OE1 A:GLN91 4.9 27.2 1.0

Potassium binding site 2 out of 4 in 8cfe

Go back to Potassium Binding Sites List in 8cfe
Potassium binding site 2 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K503

b:30.9
occ:1.00
O B:HOH798 2.8 32.1 1.0
O B:HIS382 2.8 31.4 1.0
O B:THR380 2.8 28.5 1.0
OG1 B:THR380 2.8 28.1 1.0
O B:HOH725 2.9 26.2 1.0
O A:HOH783 3.0 27.6 1.0
OE1 B:GLN65 3.3 29.1 1.0
NE2 B:GLN65 3.5 27.5 1.0
CB B:THR380 3.5 34.0 1.0
CD B:GLN65 3.5 28.6 1.0
C B:HIS382 3.6 26.6 1.0
C B:THR380 3.6 29.7 1.0
O B:GLY381 3.8 29.0 1.0
CA B:PRO383 4.0 27.1 1.0
C B:GLY381 4.1 32.9 1.0
N6 B:ADE502 4.1 31.2 1.0
N B:PRO383 4.1 29.5 1.0
CA B:THR380 4.2 31.3 1.0
CB A:ASP216 4.3 26.1 1.0
O B:HOH844 4.4 37.2 1.0
N B:HIS382 4.4 29.2 1.0
N B:GLY381 4.6 28.4 1.0
CG A:ASP216 4.6 31.3 1.0
CA B:HIS382 4.6 28.1 1.0
CG B:GLN65 4.7 31.8 1.0
OD1 A:ASP216 4.7 28.8 1.0
C B:PRO383 4.7 28.0 1.0
CA B:GLY381 4.8 33.8 1.0
N B:SER384 4.8 28.2 1.0
CG2 B:THR380 4.8 32.6 1.0
O A:ASP216 4.9 29.3 1.0
OE1 B:GLN91 4.9 34.5 1.0
O A:HOH936 5.0 41.3 1.0

Potassium binding site 3 out of 4 in 8cfe

Go back to Potassium Binding Sites List in 8cfe
Potassium binding site 3 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K505

b:27.8
occ:1.00
O C:THR380 2.7 26.1 1.0
O C:HIS382 2.8 26.7 1.0
OG1 C:THR380 2.8 26.4 1.0
O C:HOH768 2.8 25.2 1.0
O C:HOH747 2.9 31.0 1.0
O D:HOH696 3.1 27.9 1.0
OE1 C:GLN65 3.2 27.0 1.0
CD C:GLN65 3.5 25.6 1.0
NE2 C:GLN65 3.5 25.8 1.0
CB C:THR380 3.5 28.8 1.0
C C:THR380 3.6 27.7 1.0
C C:HIS382 3.6 28.2 1.0
O C:GLY381 3.8 27.1 1.0
CA C:PRO383 4.0 27.5 1.0
N6 C:ADE502 4.1 30.2 1.0
C C:GLY381 4.1 28.2 1.0
CA C:THR380 4.2 27.2 1.0
N C:PRO383 4.2 27.7 1.0
CB D:ASP216 4.3 27.3 1.0
N C:HIS382 4.4 26.3 1.0
N C:GLY381 4.5 26.1 1.0
CG D:ASP216 4.6 31.9 1.0
CG C:GLN65 4.6 23.9 1.0
O C:HOH892 4.6 33.1 1.0
OD1 D:ASP216 4.7 30.8 1.0
CA C:HIS382 4.7 28.8 1.0
CA C:GLY381 4.7 24.8 1.0
C C:PRO383 4.8 27.9 1.0
OE1 C:GLN91 4.8 30.3 1.0
CG2 C:THR380 4.8 26.6 1.0
N C:SER384 4.8 26.1 1.0
O D:ASP216 4.9 27.4 1.0

Potassium binding site 4 out of 4 in 8cfe

Go back to Potassium Binding Sites List in 8cfe
Potassium binding site 4 out of 4 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B03 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K504

b:25.5
occ:1.00
O D:THR380 2.7 27.4 1.0
O D:HIS382 2.7 26.4 1.0
O D:HOH792 2.8 27.9 1.0
OG1 D:THR380 2.8 24.8 1.0
O D:HOH778 2.9 26.2 1.0
O C:HOH795 3.1 27.0 1.0
OE1 D:GLN65 3.2 25.7 1.0
NE2 D:GLN65 3.5 23.0 1.0
CB D:THR380 3.5 26.4 1.0
CD D:GLN65 3.5 25.1 1.0
C D:THR380 3.5 24.4 1.0
C D:HIS382 3.6 22.3 1.0
O D:GLY381 3.8 25.7 1.0
CA D:PRO383 4.0 23.8 1.0
N6 D:ADE502 4.0 26.7 1.0
C D:GLY381 4.0 23.6 1.0
N D:PRO383 4.2 23.7 1.0
CA D:THR380 4.2 22.6 1.0
CB C:ASP216 4.3 25.2 1.0
N D:HIS382 4.4 24.6 1.0
N D:GLY381 4.5 24.8 1.0
CG C:ASP216 4.6 29.1 1.0
O D:HOH914 4.6 33.8 1.0
OD1 C:ASP216 4.6 26.4 1.0
CA D:HIS382 4.7 23.6 1.0
CG D:GLN65 4.7 25.0 1.0
CA D:GLY381 4.7 22.9 1.0
C D:PRO383 4.7 25.5 1.0
N D:SER384 4.8 23.3 1.0
CG2 D:THR380 4.8 25.4 1.0
OE1 D:GLN91 4.9 28.7 1.0
O C:ASP216 5.0 27.6 1.0

Reference:

P.H.Malecki, M.Gawel, M.Stepniewska, K.Brzezinski. Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with Fragment F2X-Entry B03 To Be Published.
Page generated: Mon Aug 12 22:25:59 2024

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