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Potassium in PDB 8cft: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment G12

Enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment G12

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment G12:
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 G12, PDB code: 8cft 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) 29.32 / 1.72
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 175.03, 104.14, 107.38, 90, 100.59, 90
R / Rfree (%) 15.6 / 18.7

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 G12 (pdb code 8cft). 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 G12, PDB code: 8cft:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 8cft

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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 G12


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 G12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:22.9
occ:1.00
O A:THR380 2.7 21.3 1.0
OG1 A:THR380 2.7 21.3 1.0
O A:HIS382 2.8 21.3 1.0
O A:HOH852 2.8 22.9 1.0
O A:HOH807 2.8 22.7 1.0
O B:HOH811 3.0 24.1 1.0
OE1 A:GLN65 3.2 23.7 1.0
NE2 A:GLN65 3.4 21.2 1.0
CB A:THR380 3.4 22.9 1.0
CD A:GLN65 3.5 22.9 1.0
C A:THR380 3.6 21.3 1.0
C A:HIS382 3.7 19.0 1.0
O A:GLY381 3.8 21.6 1.0
CA A:PRO383 4.0 19.9 1.0
N6 A:ADE502 4.1 21.0 1.0
C A:GLY381 4.1 23.7 1.0
CA A:THR380 4.2 22.3 1.0
N A:PRO383 4.2 20.1 1.0
CB B:ASP216 4.3 22.3 1.0
CG B:ASP216 4.5 24.6 1.0
O A:HOH950 4.5 29.5 1.0
N A:HIS382 4.5 20.9 1.0
N A:GLY381 4.5 20.7 1.0
OD1 B:ASP216 4.6 24.8 1.0
CG A:GLN65 4.6 24.5 1.0
C A:PRO383 4.7 22.1 1.0
CA A:HIS382 4.7 23.2 1.0
CG2 A:THR380 4.7 22.8 1.0
N A:SER384 4.8 22.2 1.0
CA A:GLY381 4.8 22.9 1.0
OE1 A:GLN91 4.9 24.3 1.0
O B:ASP216 5.0 24.0 1.0

Potassium binding site 2 out of 4 in 8cft

Go back to Potassium Binding Sites List in 8cft
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 G12


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 G12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K503

b:25.7
occ:1.00
O B:THR380 2.7 22.7 1.0
OG1 B:THR380 2.7 24.1 1.0
O B:HIS382 2.8 23.8 1.0
O B:HOH842 2.8 28.3 1.0
O B:HOH692 2.8 23.7 1.0
O A:HOH815 3.0 24.4 1.0
OE1 B:GLN65 3.3 24.0 1.0
NE2 B:GLN65 3.4 22.6 1.0
CB B:THR380 3.5 27.0 1.0
CD B:GLN65 3.5 25.8 1.0
C B:THR380 3.6 24.1 1.0
C B:HIS382 3.6 24.6 1.0
O B:GLY381 3.7 22.6 1.0
CA B:PRO383 4.0 22.4 1.0
N6 B:ADE502 4.0 25.1 1.0
C B:GLY381 4.1 28.1 1.0
N B:PRO383 4.2 21.6 1.0
CA B:THR380 4.2 24.9 1.0
CB A:ASP216 4.3 24.2 1.0
O B:HOH904 4.4 30.2 1.0
N B:HIS382 4.5 25.3 1.0
N B:GLY381 4.5 24.7 1.0
CG A:ASP216 4.6 26.4 1.0
CG B:GLN65 4.7 23.6 1.0
CA B:HIS382 4.7 27.2 1.0
C B:PRO383 4.7 24.5 1.0
OD1 A:ASP216 4.7 24.2 1.0
CG2 B:THR380 4.7 25.1 1.0
N B:SER384 4.8 23.3 1.0
CA B:GLY381 4.8 26.1 1.0
OE1 B:GLN91 4.9 27.9 1.0
O A:ASP216 5.0 23.5 1.0

Potassium binding site 3 out of 4 in 8cft

Go back to Potassium Binding Sites List in 8cft
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 G12


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 G12 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K504

b:26.1
occ:1.00
O C:THR380 2.8 25.9 1.0
O C:HIS382 2.8 24.7 1.0
O C:HOH736 2.8 23.9 1.0
O C:HOH726 2.8 28.3 1.0
OG1 C:THR380 2.8 24.8 1.0
O D:HOH672 3.0 25.8 1.0
OE1 C:GLN65 3.1 24.7 1.0
NE2 C:GLN65 3.4 23.7 1.0
CD C:GLN65 3.4 27.0 1.0
CB C:THR380 3.5 26.8 1.0
C C:HIS382 3.6 24.5 1.0
C C:THR380 3.6 23.6 1.0
O C:GLY381 3.8 25.4 1.0
CA C:PRO383 4.0 22.8 1.0
N6 C:ADE502 4.0 26.9 1.0
C C:GLY381 4.1 29.8 1.0
N C:PRO383 4.2 25.2 1.0
CA C:THR380 4.3 22.4 1.0
CB D:ASP216 4.3 25.2 1.0
O C:HOH924 4.5 30.3 1.0
N C:HIS382 4.5 26.9 1.0
N C:GLY381 4.6 24.7 1.0
CG C:GLN65 4.6 23.8 1.0
CG D:ASP216 4.6 27.9 1.0
OD1 D:ASP216 4.7 26.5 1.0
C C:PRO383 4.7 24.9 1.0
CA C:HIS382 4.7 25.9 1.0
CA C:GLY381 4.8 27.5 1.0
N C:SER384 4.8 27.3 1.0
CG2 C:THR380 4.8 26.5 1.0
OE1 C:GLN91 4.9 28.9 1.0
O D:ASP216 4.9 25.6 1.0

Potassium binding site 4 out of 4 in 8cft

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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 G12


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 G12 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K506

b:23.0
occ:0.95
O D:THR380 2.7 25.1 1.0
O D:HIS382 2.8 24.0 1.0
O D:HOH827 2.8 21.2 1.0
OG1 D:THR380 2.8 25.2 1.0
O D:HOH774 2.9 23.6 1.0
O C:HOH822 3.1 24.4 1.0
OE1 D:GLN65 3.2 24.1 1.0
CB D:THR380 3.5 24.4 1.0
NE2 D:GLN65 3.5 22.1 1.0
CD D:GLN65 3.5 26.3 1.0
C D:THR380 3.6 25.7 1.0
C D:HIS382 3.6 20.8 1.0
O D:GLY381 3.7 23.6 1.0
CA D:PRO383 4.0 21.6 1.0
N6 D:ADE502 4.1 26.0 1.0
C D:GLY381 4.1 26.6 1.0
N D:PRO383 4.1 22.1 1.0
CA D:THR380 4.2 21.0 1.0
CB C:ASP216 4.3 23.8 1.0
N D:HIS382 4.4 24.1 1.0
O D:HOH933 4.5 28.8 1.0
CG C:ASP216 4.5 27.4 1.0
N D:GLY381 4.5 24.0 1.0
OD1 C:ASP216 4.6 27.5 1.0
CA D:HIS382 4.6 22.9 1.0
CG D:GLN65 4.7 24.1 1.0
C D:PRO383 4.7 25.5 1.0
CA D:GLY381 4.8 23.1 1.0
CG2 D:THR380 4.8 23.7 1.0
OE1 D:GLN91 4.8 29.3 1.0
N D:SER384 4.8 25.4 1.0
O C:ASP216 5.0 22.3 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 G12 To Be Published.
Page generated: Mon Aug 12 22:33:10 2024

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