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Potassium in PDB 4aop: Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound

Enzymatic activity of Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound

All present enzymatic activity of Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound:
1.8.1.2;

Protein crystallography data

The structure of Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound, PDB code: 4aop 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 (%) 17.5 / n/a

Other elements in 4aop:

The structure of Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound (pdb code 4aop). 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 Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound, PDB code: 4aop:

Potassium binding site 1 out of 1 in 4aop

Go back to Potassium Binding Sites List in 4aop
Potassium binding site 1 out of 1 in the Sulfite Reductase Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially 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 Hemoprotein Partially Photoreduced with Proflavine Edta, Phosphate Partially Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K590

b:24.1
occ:1.00
 OD1 A:ASN397 2.7 15.1 1.0
O A:ILE362 2.7 14.3 1.0
O A:ASN395 2.8 15.5 1.0
O A:HOH789 3.0 32.8 1.0
O A:HOH647 3.1 18.7 1.0
O A:HOH614 3.2 20.7 1.0
O A:GLN396 3.4 16.1 1.0
CG A:ASN397 3.4 13.6 1.0
ND2 A:ASN397 3.8 13.7 1.0
C A:GLN396 3.8 14.9 1.0
C A:ILE362 3.8 16.2 1.0
CE1 A:PHE361 4.0 15.1 1.0
C A:ASN395 4.0 14.0 1.0
CB A:GLN396 4.0 12.3 1.0
N A:ASN364 4.1 15.6 1.0
CD1 A:PHE361 4.2 16.6 1.0
N A:GLY365 4.2 14.3 1.0
CA A:GLN396 4.3 12.2 1.0
OE1 A:GLN396 4.3 14.4 1.0
N A:ASN397 4.3 14.8 1.0
N A:ILE362 4.3 18.6 1.0
CA A:GLU363 4.6 18.6 1.0
N A:GLN396 4.6 11.8 1.0
N A:GLU363 4.6 16.9 1.0
CB A:ASN397 4.6 12.3 1.0
CA A:ASN397 4.6 15.7 1.0
C A:GLU363 4.7 18.0 1.0
CA A:ILE362 4.7 16.3 1.0
CA A:ASN364 4.7 16.4 1.0
CZ A:PHE361 4.8 14.7 1.0
C A:ASN364 4.9 16.0 1.0
O A:HOH618 5.0 18.0 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 10:03:20 2024

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