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Potassium in PDB 2b1g: Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase

Enzymatic activity of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase

All present enzymatic activity of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase:
2.1.2.3; 3.5.4.10;

Protein crystallography data

The structure of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase, PDB code: 2b1g was solved by L.Xu, Y.Chong, I.Hwang, A.D'onofrio, K.Amore, G.P.Beardsley, C.Li, A.J.Olson, D.L.Boger, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.89 / 2.10
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 57.200, 62.000, 196.600, 80.80, 81.50, 90.00
R / Rfree (%) 19.9 / 24.8

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase (pdb code 2b1g). 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 Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase, PDB code: 2b1g:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 2b1g

Go back to Potassium Binding Sites List in 2b1g
Potassium binding site 1 out of 4 in the Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1001

b:27.6
occ:1.00
 O A:VAL426 2.6 23.9 1.0
O A:THR429 2.7 26.5 1.0
OD2 A:ASP540 2.8 31.9 1.0
O A:LEU590 2.8 25.7 1.0
OG A:SER433 2.9 28.0 1.0
OG A:SER431 2.9 25.2 1.0
CB A:HIS592 3.7 30.4 1.0
N A:HIS592 3.7 29.9 1.0
CG A:ASP540 3.7 29.5 1.0
C A:VAL426 3.8 24.0 1.0
C A:THR429 3.8 25.5 1.0
CB A:ASP540 3.9 29.0 1.0
C A:LEU590 3.9 26.6 1.0
CB A:SER433 4.1 28.6 1.0
CB A:SER431 4.1 27.8 1.0
C A:PHE591 4.1 28.9 1.0
CA A:PHE591 4.2 28.2 1.0
N A:THR429 4.2 25.1 1.0
CA A:SER431 4.3 27.9 1.0
CA A:HIS592 4.3 30.8 1.0
N A:SER431 4.3 27.0 1.0
C A:GLN430 4.4 27.6 1.0
CB A:THR429 4.5 24.2 1.0
CA A:THR429 4.5 24.9 1.0
O A:LYS427 4.5 22.9 1.0
CG1 A:VAL426 4.5 25.6 1.0
O A:GLN430 4.5 27.6 1.0
N A:PHE591 4.6 27.8 1.0
C A:LYS427 4.6 23.2 1.0
CA A:VAL426 4.6 23.6 1.0
N A:LYS427 4.7 24.3 1.0
CA A:LYS427 4.7 22.8 1.0
O A:HIS592 4.8 32.0 1.0
N A:GLN430 4.9 26.4 1.0
OD1 A:ASP540 4.9 30.4 1.0
CG A:HIS592 4.9 33.9 1.0
N A:SER433 4.9 28.0 1.0
O A:PHE591 4.9 27.7 1.0
CB A:LEU590 4.9 26.2 1.0
CA A:GLN430 5.0 27.0 1.0

Potassium binding site 2 out of 4 in 2b1g

Go back to Potassium Binding Sites List in 2b1g
Potassium binding site 2 out of 4 in the Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1002

b:33.8
occ:1.00
 O B:VAL426 2.6 33.3 1.0
O B:THR429 2.6 28.3 1.0
O B:LEU590 2.7 33.3 1.0
OG B:SER431 3.0 31.4 1.0
OG B:SER433 3.1 35.1 1.0
OD2 B:ASP540 3.2 39.0 1.0
CB B:HIS592 3.6 33.0 1.0
C B:VAL426 3.8 32.8 1.0
C B:THR429 3.8 27.9 1.0
N B:HIS592 3.8 32.4 1.0
CB B:ASP540 3.8 35.0 1.0
C B:LEU590 3.9 34.1 1.0
CB B:SER433 3.9 34.2 1.0
CG B:ASP540 4.0 37.1 1.0
C B:PHE591 4.1 32.8 1.0
CA B:PHE591 4.2 33.0 1.0
CB B:SER431 4.3 31.2 1.0
N B:SER431 4.3 30.6 1.0
N B:THR429 4.3 28.1 1.0
CA B:HIS592 4.3 32.9 1.0
CA B:SER431 4.4 31.3 1.0
CG1 B:VAL426 4.4 32.2 1.0
O B:LYS427 4.4 29.8 1.0
CA B:THR429 4.4 27.7 1.0
C B:LYS427 4.5 30.9 1.0
CB B:THR429 4.5 27.5 1.0
N B:PHE591 4.5 33.6 1.0
C B:GLN430 4.5 30.2 1.0
CA B:LYS427 4.6 31.6 1.0
N B:LYS427 4.6 32.3 1.0
CA B:VAL426 4.7 32.7 1.0
N B:GLN430 4.8 28.4 1.0
O B:HIS592 4.8 32.3 1.0
CB B:LEU590 4.9 35.0 1.0
O B:PHE591 4.9 33.0 1.0
CG B:HIS592 4.9 34.0 1.0
N B:SER433 4.9 34.6 1.0
O B:GLN430 4.9 31.4 1.0
CA B:GLN430 5.0 29.7 1.0
N B:TYR428 5.0 30.2 1.0

Potassium binding site 3 out of 4 in 2b1g

Go back to Potassium Binding Sites List in 2b1g
Potassium binding site 3 out of 4 in the Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1003

b:33.3
occ:1.00
 O C:VAL426 2.6 32.2 1.0
O C:THR429 2.7 28.7 1.0
O C:LEU590 2.7 32.1 1.0
OD2 C:ASP540 2.9 37.6 1.0
OG C:SER433 3.0 36.1 1.0
OG C:SER431 3.1 31.9 1.0
CB C:HIS592 3.7 33.0 1.0
C C:VAL426 3.8 31.9 1.0
CG C:ASP540 3.8 35.3 1.0
C C:THR429 3.8 29.2 1.0
CB C:SER433 3.8 32.0 1.0
CB C:ASP540 3.9 34.2 1.0
N C:HIS592 3.9 31.1 1.0
C C:LEU590 3.9 31.9 1.0
C C:PHE591 4.1 30.7 1.0
CA C:PHE591 4.2 30.7 1.0
N C:THR429 4.3 29.8 1.0
N C:SER431 4.3 30.7 1.0
CB C:SER431 4.3 31.6 1.0
CA C:HIS592 4.4 32.2 1.0
CA C:SER431 4.4 31.8 1.0
CG1 C:VAL426 4.5 33.9 1.0
CA C:THR429 4.5 29.3 1.0
O C:LYS427 4.5 29.4 1.0
CB C:THR429 4.5 29.6 1.0
C C:LYS427 4.5 30.5 1.0
N C:PHE591 4.5 30.7 1.0
C C:GLN430 4.5 30.6 1.0
CA C:VAL426 4.6 32.1 1.0
N C:LYS427 4.6 31.7 1.0
CA C:LYS427 4.7 31.2 1.0
O C:PHE591 4.8 30.1 1.0
O C:HIS592 4.8 32.5 1.0
N C:GLN430 4.8 29.8 1.0
N C:SER433 4.9 33.6 1.0
CG C:HIS592 4.9 33.2 1.0
CB C:LEU590 4.9 32.6 1.0
O C:GLN430 4.9 30.6 1.0
OD1 C:ASP540 5.0 37.4 1.0
CA C:SER433 5.0 33.0 1.0

Potassium binding site 4 out of 4 in 2b1g

Go back to Potassium Binding Sites List in 2b1g
Potassium binding site 4 out of 4 in the Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1004

b:26.8
occ:1.00
 O D:VAL426 2.6 24.1 1.0
O D:THR429 2.7 27.1 1.0
O D:LEU590 2.7 25.6 1.0
OG D:SER433 2.9 27.7 1.0
OG D:SER431 3.1 27.9 1.0
OD2 D:ASP540 3.1 34.2 1.0
CB D:HIS592 3.6 28.8 1.0
N D:HIS592 3.7 28.7 1.0
C D:VAL426 3.8 24.2 1.0
CB D:ASP540 3.8 27.8 1.0
C D:THR429 3.9 27.3 1.0
C D:LEU590 3.9 26.7 1.0
CG D:ASP540 3.9 30.3 1.0
C D:PHE591 4.2 29.0 1.0
CB D:SER431 4.2 28.6 1.0
CA D:HIS592 4.3 29.5 1.0
N D:THR429 4.3 27.5 1.0
CB D:SER433 4.3 29.2 1.0
CA D:PHE591 4.3 28.5 1.0
CG1 D:VAL426 4.3 25.3 1.0
O D:LYS427 4.3 24.1 1.0
N D:SER431 4.3 27.5 1.0
CA D:SER431 4.4 28.8 1.0
C D:LYS427 4.5 24.8 1.0
CA D:THR429 4.5 26.8 1.0
CB D:THR429 4.5 26.6 1.0
N D:PHE591 4.5 28.0 1.0
C D:GLN430 4.6 27.4 1.0
N D:LYS427 4.6 24.2 1.0
CA D:VAL426 4.6 24.0 1.0
CA D:LYS427 4.7 23.9 1.0
O D:HIS592 4.7 28.2 1.0
CG D:HIS592 4.8 31.7 1.0
CB D:LEU590 4.8 25.5 1.0
O D:GLN430 4.9 28.0 1.0
N D:GLN430 4.9 26.9 1.0
O D:PHE591 4.9 28.6 1.0
N D:SER433 5.0 28.9 1.0

Reference:

L.Xu, Y.Chong, I.Hwang, A.D'onofrio, K.Amore, G.P.Beardsley, C.Li, A.J.Olson, D.L.Boger, I.A.Wilson. Structure-Based Design, Synthesis, Evaluation, and Crystal Structures of Transition State Analogue Inhibitors of Inosine Monophosphate Cyclohydrolase. J.Biol.Chem. V. 282 13033 2007.
ISSN: ISSN 0021-9258
PubMed: 17324932
DOI: 10.1074/JBC.M607293200
Page generated: Mon Aug 12 06:03:08 2024

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