Sodium in PDB 7oey: Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution

All present enzymatic activity of Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution:
2.2.1.2;

The structure of Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution, PDB code: 7oey was solved by F.Rabe Von Pappenheim, M.Wensien, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.88 / 1.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	172.4, 55.04, 84.37, 90, 108.69, 90
R / Rfree (%)	13.6 / 16.2

The binding sites of Sodium atom in the Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution (pdb code 7oey). 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 Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution, PDB code: 7oey:

Sodium binding site 1 out of 1 in the Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Neisseria Gonnorhoeae Variant E93Q at 1.35 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Na404 b:47.5 occ:1.00 OE1 B:GLU234 2.3 28.2 1.0 O B:HOH807 2.3 49.6 1.0 OE1 B:GLN231 2.4 23.4 1.0 O B:HOH731 2.4 25.4 0.7 O B:HOH943 3.1 49.8 0.5 CD B:GLN231 3.4 21.4 1.0 CD B:GLU234 3.5 25.7 1.0 HB2 B:GLU234 3.7 22.9 1.0 O B:HOH654 3.7 39.4 1.0 HE22 B:GLN231 3.8 27.2 1.0 HA B:GLN231 3.9 20.2 1.0 O B:HOH645 4.0 27.9 1.0 HE21 B:GLN235 4.0 33.3 0.3 O B:HOH849 4.0 34.1 1.0 NE2 B:GLN231 4.0 22.6 1.0 HB3 B:GLU234 4.1 22.9 1.0 HB3 B:GLN231 4.1 22.0 1.0 OE2 B:GLU234 4.2 26.9 1.0 CB B:GLU234 4.2 19.1 1.0 HG3 B:GLN235 4.3 28.2 0.3 CG B:GLU234 4.5 21.2 1.0 CG B:GLN231 4.6 18.4 1.0 CB B:GLN231 4.6 18.3 1.0 CA B:GLN231 4.6 16.8 1.0 O B:GLN231 4.7 16.8 1.0 NE2 B:GLN235 4.8 27.8 0.3 HE21 B:GLN231 4.8 27.2 1.0 HG3 B:GLU234 4.9 25.4 1.0 HG3 B:GLN231 5.0 22.1 1.0

F.Rabe Von Pappenheim, M.Wensien, J.Ye, J.Uranga, I.Irisarri, J.De Vries, L.M.Funk, R.A.Mata, K.Tittmann. Widespread Occurrence of Covalent Lysine-Cysteine Redox Switches in Proteins. Nat.Chem.Biol. V. 18 368 2022.
ISSN: ESSN 1552-4469
PubMed: 35165445
DOI: 10.1038/S41589-021-00966-5