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Potassium in PDB 1g8m: Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution

Enzymatic activity of Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution

All present enzymatic activity of Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution:
2.1.2.3; 3.5.4.10;

Protein crystallography data

The structure of Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution, PDB code: 1g8m was solved by S.E.Greasley, P.Horton, G.P.Beardsley, S.J.Benkovic, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 65.100, 106.000, 103.500, 90.00, 108.00, 90.00
R / Rfree (%) 20 / 21.6

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution (pdb code 1g8m). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution, PDB code: 1g8m:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1g8m

Go back to Potassium Binding Sites List in 1g8m
Potassium binding site 1 out of 2 in the Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution


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 Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1001

b:10.9
occ:1.00
 O A:THR429 2.8 7.6 1.0
O A:LEU590 2.8 9.1 1.0
O A:VAL426 2.8 8.4 1.0
OG A:SER433 2.8 17.4 1.0
OG A:SER431 3.0 11.6 1.0
OD1 A:ASP540 3.1 15.2 1.0
N A:HIS592 3.7 9.2 1.0
CB A:HIS592 3.7 10.2 1.0
CB A:ASP540 3.8 10.9 1.0
C A:THR429 3.9 8.4 1.0
CG A:ASP540 3.9 13.7 1.0
C A:VAL426 3.9 8.9 1.0
C A:LEU590 3.9 9.6 1.0
C A:PHE591 4.1 9.0 1.0
CG1 A:VAL426 4.1 9.1 1.0
CA A:PHE591 4.1 8.8 1.0
CB A:SER431 4.2 11.0 1.0
CB A:SER433 4.2 14.4 1.0
N A:SER431 4.2 9.8 1.0
CA A:SER431 4.3 10.3 1.0
N A:THR429 4.3 8.0 1.0
CA A:HIS592 4.3 9.5 1.0
CB A:THR429 4.5 9.0 1.0
CA A:THR429 4.5 7.6 1.0
C A:GLN430 4.5 9.4 1.0
N A:PHE591 4.5 8.8 1.0
C A:LYS427 4.7 7.5 1.0
N A:SER433 4.7 12.0 1.0
O A:LYS427 4.7 6.6 1.0
CA A:VAL426 4.7 8.9 1.0
N A:LYS427 4.8 8.2 1.0
CA A:LYS427 4.8 7.6 1.0
O A:HIS592 4.8 9.7 1.0
O A:PHE591 4.8 9.9 1.0
O A:GLN430 4.8 10.3 1.0
CB A:LEU590 4.9 9.3 1.0
CG A:HIS592 4.9 10.5 1.0
N A:GLN430 4.9 8.2 1.0
CB A:VAL426 5.0 9.2 1.0

Potassium binding site 2 out of 2 in 1g8m

Go back to Potassium Binding Sites List in 1g8m
Potassium binding site 2 out of 2 in the Crystal Structure of Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution


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 Avian Atic, A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis at 1.75 Ang. Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1002

b:13.0
occ:1.00
 O B:THR429 2.8 8.5 1.0
O B:VAL426 2.8 9.6 1.0
O B:LEU590 2.8 9.8 1.0
OG B:SER433 3.0 19.5 1.0
OG B:SER431 3.1 12.9 1.0
OD2 B:ASP540 3.1 18.1 1.0
N B:HIS592 3.7 9.7 1.0
CB B:HIS592 3.7 10.0 1.0
C B:THR429 3.9 9.3 1.0
CB B:ASP540 3.9 14.0 1.0
C B:VAL426 3.9 9.8 1.0
CG B:ASP540 4.0 15.8 1.0
C B:LEU590 4.0 9.7 1.0
CG1 B:VAL426 4.0 13.0 1.0
CB B:SER433 4.1 15.4 1.0
C B:PHE591 4.1 10.1 1.0
CA B:PHE591 4.2 9.8 1.0
CB B:SER431 4.2 12.0 1.0
N B:SER431 4.2 10.5 1.0
N B:THR429 4.3 9.2 1.0
CA B:SER431 4.3 11.7 1.0
CA B:HIS592 4.3 10.4 1.0
CB B:THR429 4.4 8.9 1.0
CA B:THR429 4.4 8.7 1.0
C B:GLN430 4.5 10.2 1.0
N B:PHE591 4.5 9.7 1.0
O B:LYS427 4.6 7.4 1.0
C B:LYS427 4.7 8.7 1.0
CA B:VAL426 4.7 9.9 1.0
O B:HIS592 4.8 10.1 1.0
N B:LYS427 4.8 8.8 1.0
O B:GLN430 4.8 9.1 1.0
CA B:LYS427 4.8 8.6 1.0
N B:SER433 4.9 13.9 1.0
CB B:LEU590 4.9 9.6 1.0
N B:GLN430 4.9 9.3 1.0
CG B:HIS592 4.9 11.5 1.0
O B:PHE591 4.9 10.4 1.0

Reference:

S.E.Greasley, P.Horton, J.Ramcharan, G.P.Beardsley, S.J.Benkovic, I.A.Wilson. Crystal Structure of A Bifunctional Transformylase and Cyclohydrolase Enzyme in Purine Biosynthesis. Nat.Struct.Biol. V. 8 402 2001.
ISSN: ISSN 1072-8368
PubMed: 11323713
DOI: 10.1038/87555
Page generated: Mon Aug 12 04:30:03 2024

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