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Potassium in PDB 6gep: Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta

Enzymatic activity of Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta

All present enzymatic activity of Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta:
1.8.1.2;

Protein crystallography data

The structure of Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta, PDB code: 6gep was solved by B.R.Crane, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.800, 77.400, 87.800, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / n/a

Other elements in 6gep:

The structure of Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta (pdb code 6gep). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta, PDB code: 6gep:

Potassium binding site 1 out of 1 in 6gep

Go back to Potassium Binding Sites List in 6gep
Potassium binding site 1 out of 1 in the Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Sulfite Reductase Hemoprotein Nitric Oxide Complex Reduced with Proflavine Edta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K590

b:28.0
occ:1.00
 O A:HOH917 2.4 61.1 1.0
O A:ILE362 2.7 14.7 1.0
OD1 A:ASN397 2.7 13.0 1.0
O A:ASN395 2.8 13.8 1.0
O A:HOH686 3.2 22.2 1.0
O A:GLN396 3.3 15.4 1.0
O A:HOH673 3.4 31.1 1.0
O A:HOH646 3.4 21.2 1.0
CG A:ASN397 3.5 13.4 1.0
C A:GLN396 3.7 14.2 1.0
C A:ILE362 3.7 14.8 1.0
ND2 A:ASN397 3.9 13.3 1.0
CB A:GLN396 3.9 11.4 1.0
C A:ASN395 3.9 12.3 1.0
CE1 A:PHE361 4.0 14.3 1.0
N A:ASN364 4.1 13.8 1.0
CA A:GLN396 4.2 12.1 1.0
N A:GLY365 4.2 15.0 1.0
CD1 A:PHE361 4.3 16.9 1.0
N A:ASN397 4.3 13.8 1.0
N A:ILE362 4.3 16.7 1.0
OE1 A:GLN396 4.3 14.7 1.0
N A:GLN396 4.5 12.0 1.0
N A:GLU363 4.5 16.3 1.0
CA A:GLU363 4.5 15.7 1.0
CA A:ASN397 4.6 14.6 1.0
CA A:ILE362 4.6 15.8 1.0
CB A:ASN397 4.6 12.7 1.0
C A:GLU363 4.7 15.4 1.0
CA A:ASN364 4.8 15.6 1.0
CZ A:PHE361 4.8 14.4 1.0
C A:ASN364 4.9 15.9 1.0
O A:HOH623 4.9 17.8 1.0
CA A:GLY365 4.9 14.7 1.0

Reference:

B.R.Crane, L.M.Siegel, E.D.Getzoff. Probing the Catalytic Mechanism of Sulfite Reductase By X-Ray Crystallography: Structures of the Escherichia Coli Hemoprotein in Complex with Substrates, Inhibitors, Intermediates, and Products. Biochemistry V. 36 12120 1997.
ISSN: ISSN 0006-2960
PubMed: 9315849
DOI: 10.1021/BI971066I
Page generated: Mon Aug 12 16:08:40 2024

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