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Potassium in PDB 5gep: Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii Edta

Enzymatic activity of Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii Edta

All present enzymatic activity of Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii Edta:
1.8.1.2;

Protein crystallography data

The structure of Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii Edta, PDB code: 5gep 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 / 2.10
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 (%) 18.4 / n/a

Other elements in 5gep:

The structure of Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii 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 Carbon Monoxide Complex Reduced with Crii Edta (pdb code 5gep). 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 Carbon Monoxide Complex Reduced with Crii Edta, PDB code: 5gep:

Potassium binding site 1 out of 1 in 5gep

Go back to Potassium Binding Sites List in 5gep
Potassium binding site 1 out of 1 in the Sulfite Reductase Hemoprotein Carbon Monoxide Complex Reduced with Crii 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 Carbon Monoxide Complex Reduced with Crii Edta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K590

b:26.0
occ:1.00
 O A:ILE362 2.7 9.8 1.0
OD1 A:ASN397 2.8 7.1 1.0
O A:HOH631 2.9 12.3 1.0
O A:ASN395 2.9 7.7 1.0
O A:HOH716 2.9 26.9 1.0
O A:HOH608 3.1 10.2 1.0
O A:GLN396 3.4 7.8 1.0
CG A:ASN397 3.5 3.1 1.0
ND2 A:ASN397 3.6 2.0 1.0
C A:ILE362 3.7 8.4 1.0
CE1 A:PHE361 3.8 7.0 1.0
C A:GLN396 3.8 9.5 1.0
CB A:GLN396 4.0 8.0 1.0
CD1 A:PHE361 4.1 8.8 1.0
C A:ASN395 4.1 5.6 1.0
N A:ASN364 4.2 8.8 1.0
N A:ILE362 4.2 11.9 1.0
OE1 A:GLN396 4.4 5.8 1.0
CA A:GLN396 4.4 8.0 1.0
N A:GLU363 4.5 8.7 1.0
N A:GLY365 4.5 10.8 1.0
N A:ASN397 4.5 10.5 1.0
CA A:GLU363 4.5 8.4 1.0
CA A:ILE362 4.5 9.6 1.0
CZ A:PHE361 4.7 9.1 1.0
CB A:ASN397 4.7 4.7 1.0
N A:GLN396 4.7 5.2 1.0
C A:GLU363 4.7 6.8 1.0
CA A:ASN397 4.8 7.2 1.0
O A:HOH606 5.0 14.3 1.0
CA A:ASN364 5.0 9.0 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 13:45:34 2024

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