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Potassium in PDB 8cfp: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment F09

Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment F09

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment F09:
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 F09, PDB code: 8cfp 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) 48.44 / 1.61
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.83, 132.89, 98.71, 90, 101.06, 90
R / Rfree (%) 15.8 / 18.9

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 F09 (pdb code 8cfp). 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 F09, PDB code: 8cfp:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 8cfp

Go back to Potassium Binding Sites List in 8cfp
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 F09


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 F09 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K506

b:18.6
occ:1.00
O A:THR380 2.6 18.8 1.0
O A:HIS382 2.7 17.1 1.0
OG1 A:THR380 2.8 18.4 1.0
O A:HOH685 2.8 16.8 1.0
O A:HOH851 2.8 16.8 1.0
O B:HOH788 3.1 16.4 1.0
OE1 A:GLN65 3.2 19.1 1.0
NE2 A:GLN65 3.4 16.2 1.0
CD A:GLN65 3.5 16.3 1.0
CB A:THR380 3.5 15.6 1.0
C A:THR380 3.6 16.9 1.0
C A:HIS382 3.6 17.5 1.0
O A:GLY381 3.7 17.3 1.0
N6 A:ADE502 4.0 16.9 1.0
CA A:PRO383 4.0 16.9 1.0
C A:GLY381 4.0 16.9 1.0
N A:PRO383 4.2 18.8 1.0
CA A:THR380 4.2 17.0 1.0
CB B:ASP216 4.3 16.4 1.0
O A:HOH906 4.4 23.0 1.0
N A:HIS382 4.4 17.0 1.0
N A:GLY381 4.5 17.0 1.0
CG A:GLN65 4.6 16.5 1.0
CG B:ASP216 4.6 17.2 1.0
CA A:HIS382 4.7 18.3 1.0
CA A:GLY381 4.7 15.8 1.0
OD1 B:ASP216 4.7 17.2 1.0
C A:PRO383 4.7 18.4 1.0
OE1 A:GLN91 4.8 20.2 1.0
N A:SER384 4.8 17.7 1.0
CG2 A:THR380 4.8 14.7 1.0
O B:ASP216 5.0 17.8 1.0

Potassium binding site 2 out of 4 in 8cfp

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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 F09


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 F09 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K508

b:16.8
occ:1.00
O B:THR380 2.7 16.0 1.0
O B:HOH750 2.8 18.0 1.0
O B:HIS382 2.8 16.4 1.0
OG1 B:THR380 2.8 17.2 1.0
O B:HOH815 2.8 15.6 1.0
O A:HOH781 3.1 18.5 1.0
OE1 B:GLN65 3.2 17.3 1.0
CB B:THR380 3.4 15.3 1.0
NE2 B:GLN65 3.4 17.6 1.0
CD B:GLN65 3.5 17.3 1.0
C B:THR380 3.6 17.3 1.0
C B:HIS382 3.6 17.7 1.0
O B:GLY381 3.8 17.1 1.0
CA B:PRO383 4.0 15.7 1.0
C B:GLY381 4.1 16.6 1.0
N6 B:ADE503 4.1 20.3 1.0
CA B:THR380 4.2 17.5 1.0
N B:PRO383 4.2 15.1 1.0
CB A:ASP216 4.3 17.9 1.0
O B:HOH933 4.4 17.8 1.0
N B:HIS382 4.5 16.7 1.0
CG A:ASP216 4.5 20.0 1.0
N B:GLY381 4.6 14.9 1.0
OD1 A:ASP216 4.6 18.1 1.0
CG B:GLN65 4.7 16.3 1.0
C B:PRO383 4.7 16.9 1.0
CA B:HIS382 4.7 17.3 1.0
CA B:GLY381 4.7 16.4 1.0
CG2 B:THR380 4.7 17.6 1.0
N B:SER384 4.7 17.6 1.0
OE1 B:GLN91 4.8 18.0 1.0
O A:ASP216 5.0 16.2 1.0

Potassium binding site 3 out of 4 in 8cfp

Go back to Potassium Binding Sites List in 8cfp
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 F09


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 F09 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K504

b:19.6
occ:1.00
O C:HOH707 2.7 20.2 1.0
O C:THR380 2.8 19.6 1.0
O C:HOH705 2.8 19.3 1.0
OG1 C:THR380 2.8 20.1 1.0
O C:HIS382 2.8 17.5 1.0
O D:HOH700 3.1 20.1 1.0
OE1 C:GLN65 3.3 19.9 1.0
NE2 C:GLN65 3.4 20.0 1.0
CB C:THR380 3.5 15.9 1.0
CD C:GLN65 3.5 20.4 1.0
C C:THR380 3.6 17.4 1.0
C C:HIS382 3.7 17.1 1.0
O C:GLY381 3.8 16.3 1.0
CA C:PRO383 4.0 19.0 1.0
N6 C:ADE502 4.1 22.3 1.0
C C:GLY381 4.1 17.1 1.0
CA C:THR380 4.2 18.5 1.0
N C:PRO383 4.2 16.5 1.0
CB D:ASP216 4.2 18.6 1.0
O C:HOH903 4.5 23.3 1.0
N C:GLY381 4.5 18.4 1.0
N C:HIS382 4.5 17.2 1.0
CG D:ASP216 4.5 18.3 1.0
CG C:GLN65 4.6 20.6 1.0
OD1 D:ASP216 4.7 18.0 1.0
C C:PRO383 4.7 21.0 1.0
OE1 C:GLN91 4.7 23.1 1.0
CG2 C:THR380 4.7 17.6 1.0
CA C:HIS382 4.7 16.5 1.0
N C:SER384 4.8 17.6 1.0
CA C:GLY381 4.8 17.6 1.0
O D:ASP216 4.9 18.5 1.0

Potassium binding site 4 out of 4 in 8cfp

Go back to Potassium Binding Sites List in 8cfp
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 F09


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 F09 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K505

b:18.2
occ:1.00
O D:THR380 2.7 19.4 1.0
O D:HOH768 2.8 18.9 1.0
OG1 D:THR380 2.8 17.9 1.0
O D:HIS382 2.8 18.0 1.0
O D:HOH851 2.8 18.0 1.0
O C:HOH750 3.1 18.3 1.0
OE1 D:GLN65 3.3 19.4 1.0
NE2 D:GLN65 3.4 16.3 1.0
CB D:THR380 3.5 21.4 1.0
CD D:GLN65 3.5 19.4 1.0
C D:THR380 3.6 18.7 1.0
C D:HIS382 3.6 19.9 1.0
O D:GLY381 3.8 18.5 1.0
CA D:PRO383 4.0 17.3 1.0
N6 D:ADE502 4.1 17.9 1.0
C D:GLY381 4.1 17.2 1.0
CA D:THR380 4.2 19.5 1.0
N D:PRO383 4.2 18.1 1.0
CB C:ASP216 4.3 21.1 1.0
O D:HOH918 4.4 22.4 1.0
N D:HIS382 4.5 17.6 1.0
CG C:ASP216 4.5 21.1 1.0
OD1 C:ASP216 4.6 21.2 1.0
N D:GLY381 4.6 19.2 1.0
CG D:GLN65 4.6 18.4 1.0
CA D:HIS382 4.7 19.8 1.0
C D:PRO383 4.7 17.0 1.0
CG2 D:THR380 4.7 19.4 1.0
N D:SER384 4.8 17.8 1.0
CA D:GLY381 4.8 16.6 1.0
OE1 D:GLN91 4.8 21.5 1.0
O C:ASP216 4.9 18.2 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 F09 To Be Published.
Page generated: Sat Aug 9 16:02:47 2025

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