Potassium in PDB 3cxc: The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui

The structure of The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui, PDB code: 3cxc was solved by J.A.Ippolito, D.Wang, Z.F.Kanyo, E.M.Duffy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	213.660, 300.710, 575.370, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Magnesium	(Mg)	117 atoms
Cadmium	(Cd)	5 atoms
Chlorine	(Cl)	22 atoms
Sodium	(Na)	86 atoms

The binding sites of Potassium atom in the The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui (pdb code 3cxc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui, PDB code: 3cxc:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui within 5.0Å range: probe atom residue distance (Å) B Occ 0:K8201 b:1.0 occ:1.00 O6 0:G2102 2.8 47.6 1.0 C5 0:U2539 3.3 55.6 1.0 O4 0:U2539 3.4 56.3 1.0 O6 0:G2482 3.5 51.5 1.0 O4' 0:C2536 3.6 47.2 1.0 N7 0:G2102 3.7 50.0 1.0 N7 0:G2482 3.7 51.3 1.0 C4 0:U2539 3.7 56.1 1.0 C6 0:G2102 3.7 48.6 1.0 C7 0:SLD9500 3.7 46.5 1.0 C8 0:SLD9500 3.8 47.3 1.0 O2' 0:U2535 3.9 46.4 1.0 OP1 0:U2539 3.9 54.0 1.0 C2' 0:U2535 4.0 44.9 1.0 C4' 0:C2536 4.0 46.4 1.0 C5 0:G2102 4.0 49.3 1.0 C5' 0:C2536 4.2 45.4 1.0 C6 0:G2482 4.3 49.6 1.0 C6 0:U2539 4.3 55.9 1.0 C5 0:G2482 4.3 49.5 1.0 C5 0:SLD9500 4.4 46.5 1.0 C1' 0:C2536 4.4 48.3 1.0 O2 0:C2536 4.5 50.0 1.0 O2 0:U2535 4.8 53.5 1.0 N6 0:A2486 4.8 52.4 1.0 C8 0:G2482 4.8 49.3 1.0 C8 0:G2102 4.9 50.0 1.0 C1' 0:U2535 4.9 46.4 1.0 C2 0:C2536 4.9 50.2 1.0 C2 0:U2535 4.9 49.8 1.0 N1 0:C2536 4.9 50.6 1.0 O5' 0:C2536 4.9 45.1 1.0 O1 0:SLD9500 5.0 48.2 1.0 N3 0:U2539 5.0 55.8 1.0 N1 0:G2102 5.0 50.0 1.0

Potassium binding site 2 out of 2 in the The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Structure of An Enhanced Oxazolidinone Inhibitor Bound to the 50S Ribosomal Subunit of H. Marismortui within 5.0Å range: probe atom residue distance (Å) B Occ 0:K8202 b:92.0 occ:1.00 O 0:HOH3105 2.7 57.3 1.0 O 0:HOH3013 2.8 55.8 1.0 O4 0:U172 2.8 51.3 1.0 O4 0:U163 2.9 48.9 1.0 O 0:HOH3137 3.0 51.9 1.0 OP2 0:C162 3.4 39.4 1.0 O 0:HOH5857 3.6 74.6 1.0 O 0:HOH8716 3.6 52.3 1.0 C4 0:U172 3.7 50.2 1.0 CD L:ARG82 3.7 49.8 1.0 N3 0:U172 3.8 51.8 1.0 O 0:HOH3311 3.9 64.6 1.0 C4 0:U163 3.9 47.7 1.0 N4 0:C171 4.1 49.1 1.0 NE L:ARG82 4.4 49.0 1.0 O 0:HOH8715 4.5 46.9 1.0 C5 0:U163 4.5 46.5 1.0 OP2 0:A169 4.5 48.3 1.0 O6 0:G164 4.6 48.4 1.0 P 0:C162 4.7 40.7 1.0 N3 0:C173 4.7 47.9 1.0 CG L:ARG82 4.8 48.7 1.0 OP1 0:A169 4.9 47.2 1.0 N4 0:C173 4.9 47.6 1.0 CB L:ARG82 4.9 47.7 1.0 MG 0:MG8054 4.9 45.2 1.0

J.Zhou, A.Bhattacharjee, S.Chen, Y.Chen, E.Duffy, J.Farmer, J.Goldberg, R.Hanselmann, J.A.Ippolito, R.Lou, A.Orbin, A.Oyelere, J.Salvino, D.Springer, J.Tran, D.Wang, Y.Wu, G.Johnson. Design at the Atomic Level: Design of Biaryloxazolidinones As Potent Orally Active Antibiotics. Bioorg.Med.Chem.Lett. V. 18 6175 2008.
ISSN: ISSN 0960-894X
PubMed: 18947996
DOI: 10.1016/J.BMCL.2008.10.011