Potassium in PDB 6c3x: Wild Type Structure of Sirhp

All present enzymatic activity of Wild Type Structure of Sirhp:
1.8.1.2;

The structure of Wild Type Structure of Sirhp, PDB code: 6c3x was solved by M.E.Stroupe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.37 / 1.54
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.794, 77.317, 87.586, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 17.1

The structure of Wild Type Structure of Sirhp also contains other interesting chemical elements:

Iron

(Fe)

5 atoms

The binding sites of Potassium atom in the Wild Type Structure of Sirhp (pdb code 6c3x). 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 Wild Type Structure of Sirhp, PDB code: 6c3x:

Potassium binding site 1 out of 1 in the Wild Type Structure of Sirhp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Wild Type Structure of Sirhp within 5.0Å range: probe atom residue distance (Å) B Occ A:K602 b:11.1 occ:1.00 OD1 A:ASN397 2.6 10.2 1.0 O A:ILE362 2.7 10.6 1.0 O A:ASN395 2.8 10.4 1.0 O A:HOH826 2.9 24.0 1.0 O A:HOH991 3.0 11.2 1.0 O A:HOH971 3.2 17.4 1.0 O A:GLN396 3.4 10.6 1.0 CG A:ASN397 3.4 8.2 1.0 C A:GLN396 3.7 9.2 1.0 CE1 A:PHE361 3.7 11.4 1.0 ND2 A:ASN397 3.8 10.3 1.0 C A:ILE362 3.8 10.9 1.0 CB A:GLN396 3.9 8.0 1.0 C A:ASN395 4.0 9.2 1.0 N A:ASN364 4.1 8.6 1.0 CD1 A:PHE361 4.1 9.9 1.0 N A:GLY365 4.2 9.2 1.0 N A:ASN397 4.2 7.3 1.0 CA A:GLN396 4.2 7.2 1.0 OE1 A:GLN396 4.3 10.5 1.0 N A:ILE362 4.4 8.7 1.0 CZ A:PHE361 4.5 10.1 1.0 N A:GLN396 4.6 7.8 1.0 CA A:GLU363 4.6 10.6 1.0 CA A:ASN397 4.6 8.0 1.0 CB A:ASN397 4.6 8.1 1.0 N A:GLU363 4.7 9.6 1.0 CA A:ILE362 4.7 9.1 1.0 C A:GLU363 4.7 10.6 1.0 CA A:ASN364 4.7 10.3 1.0 C A:ASN364 4.8 9.6 1.0 O A:HOH785 4.8 10.8 1.0

M.R.Cepeda, L.Mcgarry, J.M.Pennington, J.Krzystek, M.E.Stroupe. The Role of Extended FE4S4CLUSTER Ligands in Mediating Sulfite Reductase Hemoprotein Activity. Biochim. Biophys. Acta V.1866 933 2018.
ISSN: ISSN 0006-3002
PubMed: 29852252
DOI: 10.1016/J.BBAPAP.2018.05.013