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Potassium in PDB 1m9n: Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms.

Enzymatic activity of Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms.

All present enzymatic activity of Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms.:
2.1.2.3; 3.5.4.10;

Protein crystallography data

The structure of Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms., PDB code: 1m9n was solved by D.W.Wolan, S.E.Greasly, G.P.Beardsley, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.24 / 1.93
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.480, 107.880, 103.860, 90.00, 91.20, 90.00
R / Rfree (%) 20.6 / 24.4

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms. (pdb code 1m9n). 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 the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms., PDB code: 1m9n:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1m9n

Go back to Potassium Binding Sites List in 1m9n
Potassium binding site 1 out of 2 in the Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms.


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 the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K594

b:33.0
occ:1.00
O A:THR429 2.6 5.8 1.0
OD2 A:ASP540 2.7 9.5 1.0
O A:VAL426 2.8 9.6 1.0
O A:LEU590 2.8 5.8 1.0
OG A:SER431 2.9 7.1 1.0
OG A:SER433 2.9 14.3 1.0
CG A:ASP540 3.6 10.8 1.0
CB A:HIS592 3.7 7.4 1.0
N A:HIS592 3.7 7.2 1.0
C A:THR429 3.8 7.5 1.0
CB A:ASP540 3.8 9.3 1.0
C A:VAL426 3.9 9.0 1.0
C A:LEU590 3.9 6.9 1.0
C A:PHE591 4.1 6.6 1.0
CB A:SER431 4.1 8.2 1.0
CB A:SER433 4.1 9.8 1.0
N A:THR429 4.2 6.9 1.0
CA A:PHE591 4.2 6.5 1.0
N A:SER431 4.3 7.3 1.0
CA A:SER431 4.3 8.1 1.0
CA A:HIS592 4.3 7.0 1.0
CG1 A:VAL426 4.4 11.1 1.0
CA A:THR429 4.4 7.5 1.0
CB A:THR429 4.4 8.4 1.0
C A:GLN430 4.5 7.9 1.0
O A:LYS427 4.5 7.5 1.0
O A:HOH1111 4.6 50.3 1.0
N A:PHE591 4.6 6.4 1.0
C A:LYS427 4.6 8.2 1.0
O A:HIS592 4.7 7.0 1.0
CA A:LYS427 4.7 8.0 1.0
OD1 A:ASP540 4.8 6.6 1.0
N A:LYS427 4.8 8.1 1.0
CA A:VAL426 4.8 8.8 1.0
O A:PHE591 4.8 6.1 1.0
N A:GLN430 4.8 7.5 1.0
O A:GLN430 4.9 8.2 1.0
CG A:HIS592 4.9 6.6 1.0
CB A:LEU590 4.9 7.4 1.0
N A:SER433 4.9 8.9 1.0
CA A:GLN430 5.0 7.3 1.0

Potassium binding site 2 out of 2 in 1m9n

Go back to Potassium Binding Sites List in 1m9n
Potassium binding site 2 out of 2 in the Crystal Structure of the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms.


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 the Homodimeric Bifunctional Transformylase and Cyclohydrolase Enzyme Avian Atic in Complex with Aicar and Xmp at 1.93 Angstroms. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K594

b:37.5
occ:1.00
O B:THR429 2.6 6.9 1.0
O B:LEU590 2.6 8.2 1.0
O B:VAL426 2.7 8.8 1.0
OG B:SER431 3.0 8.1 1.0
OG B:SER433 3.0 13.7 1.0
OD2 B:ASP540 3.1 10.8 1.0
CB B:HIS592 3.7 10.4 1.0
N B:HIS592 3.7 9.2 1.0
C B:THR429 3.8 7.6 1.0
C B:LEU590 3.8 8.3 1.0
CB B:ASP540 3.9 8.5 1.0
CG B:ASP540 3.9 8.8 1.0
C B:VAL426 3.9 8.1 1.0
C B:PHE591 4.1 8.6 1.0
CA B:PHE591 4.1 8.2 1.0
CB B:SER433 4.2 10.9 1.0
CB B:SER431 4.2 7.5 1.0
N B:SER431 4.3 8.2 1.0
N B:THR429 4.3 8.1 1.0
CA B:HIS592 4.4 9.7 1.0
CA B:SER431 4.4 7.9 1.0
CG1 B:VAL426 4.4 9.3 1.0
CA B:THR429 4.4 7.5 1.0
N B:PHE591 4.5 8.4 1.0
C B:GLN430 4.5 7.9 1.0
O B:LYS427 4.5 8.1 1.0
CB B:THR429 4.5 7.9 1.0
C B:LYS427 4.6 8.0 1.0
CA B:LYS427 4.7 8.0 1.0
O B:GLN430 4.7 7.6 1.0
N B:LYS427 4.7 7.8 1.0
CA B:VAL426 4.8 8.5 1.0
O B:HIS592 4.8 9.4 1.0
N B:GLN430 4.8 7.5 1.0
CB B:LEU590 4.9 7.9 1.0
CG B:HIS592 4.9 10.8 1.0
O B:PHE591 4.9 8.0 1.0
CA B:LEU590 5.0 8.5 1.0
N B:SER433 5.0 9.5 1.0

Reference:

D.W.Wolan, S.E.Greasly, G.P.Beardsley, I.A.Wilson. Structural Insights Into the Avian Aicar Transformylase Mechanism. Biochemistry V. 41 15505 2002.
ISSN: ISSN 0006-2960
PubMed: 12501179
DOI: 10.1021/BI020505X
Page generated: Mon Aug 12 04:56:07 2024

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