Sodium in PDB 6qlh: Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate

All present enzymatic activity of Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate:
2.5.1.129;

The structure of Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate, PDB code: 6qlh was solved by S.A.Marshall, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.02 / 1.57
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	142.124, 142.124, 142.124, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 19.9

The binding sites of Sodium atom in the Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate (pdb code 6qlh). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate, PDB code: 6qlh:

Sodium binding site 1 out of 1 in the Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Ubix in Complex with Reduced Fmn and Isopentyl Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:25.3 occ:1.00 OD1 A:ASN117 2.3 27.4 1.0 O A:HOH511 2.4 18.7 1.0 O A:HOH411 2.5 17.2 1.0 CG A:ASN117 3.2 34.5 1.0 O A:ALA115 3.8 13.1 1.0 ND2 A:ASN117 3.8 27.7 1.0 O A:HOH526 4.1 40.2 1.0 CA A:ASN117 4.2 11.2 1.0 CB A:ASN117 4.3 17.4 1.0 O A:CYS116 4.6 17.9 1.0 N A:ASN117 4.7 13.2 1.0 O A:HOH565 4.8 18.4 1.0 C A:CYS116 4.8 16.8 1.0 C A:ALA115 4.9 12.9 1.0

S.A.Marshall, K.A.P.Payne, K.Fisher, M.D.White, A.Ni Cheallaigh, A.Balaikaite, S.E.J.Rigby, D.Leys. The Ubix Flavin Prenyltransferase Reaction Mechanism Resembles Class I Terpene Cyclase Chemistry. Nat Commun V. 10 2357 2019.
ISSN: ESSN 2041-1723
PubMed: 31142738
DOI: 10.1038/S41467-019-10220-1