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Potassium in PDB 2aop: Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound

Enzymatic activity of Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound

All present enzymatic activity of Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound:
1.8.1.2;

Protein crystallography data

The structure of Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound, PDB code: 2aop 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 / 1.75
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 (%) 17.5 / n/a

Other elements in 2aop:

The structure of Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound (pdb code 2aop). 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: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound, PDB code: 2aop:

Potassium binding site 1 out of 1 in 2aop

Go back to Potassium Binding Sites List in 2aop
Potassium binding site 1 out of 1 in the Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Sulfite Reductase: Reduced with Crii Edta, Siroheme Feii, [4FE-4S] +1, Phosphate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K590

b:18.3
occ:1.00
 O A:HOH715 2.5 49.6 1.0
OD1 A:ASN397 2.7 10.0 1.0
O A:ASN395 2.7 9.2 1.0
O A:ILE362 2.7 10.5 1.0
O A:HOH644 2.9 13.2 1.0
O A:HOH616 3.2 12.9 1.0
O A:GLN396 3.4 10.4 1.0
CG A:ASN397 3.4 8.8 1.0
C A:GLN396 3.7 9.3 1.0
ND2 A:ASN397 3.8 9.6 1.0
C A:ILE362 3.8 12.1 1.0
C A:ASN395 3.9 7.7 1.0
CB A:GLN396 3.9 7.0 1.0
CE1 A:PHE361 4.0 13.6 1.0
N A:ASN364 4.2 10.9 1.0
CA A:GLN396 4.2 6.8 1.0
N A:ASN397 4.3 10.9 1.0
CD1 A:PHE361 4.3 14.3 1.0
N A:GLY365 4.3 11.6 1.0
OE1 A:GLN396 4.3 11.3 1.0
N A:ILE362 4.4 13.4 1.0
N A:GLN396 4.5 7.8 1.0
CA A:GLU363 4.6 13.7 1.0
N A:GLU363 4.6 12.5 1.0
CB A:ASN397 4.6 8.7 1.0
CA A:ASN397 4.6 11.6 1.0
CA A:ILE362 4.7 12.8 1.0
C A:GLU363 4.7 12.5 1.0
CZ A:PHE361 4.8 13.5 1.0
CA A:ASN364 4.8 11.5 1.0
O A:HOH627 4.9 12.9 1.0
C A:ASN364 4.9 12.2 1.0

Reference:

B.R.Crane, L.M.Siegel, E.D.Getzoff. Structures of the Siroheme- and FE4S4-Containing Active Center of Sulfite Reductase in Different States of Oxidation: Heme Activation Via Reduction-Gated Exogenous Ligand Exchange. Biochemistry V. 36 12101 1997.
ISSN: ISSN 0006-2960
PubMed: 9315848
DOI: 10.1021/BI971065Q
Page generated: Mon Aug 12 06:01:55 2024

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