Sodium in PDB 7qf7: Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin

The structure of Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin, PDB code: 7qf7 was solved by M.S.Semrau, P.Storici, G.Lolli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.07 / 1.47
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.593, 56.443, 70.553, 90, 90, 90
R / Rfree (%)	17.6 / 19.5

The binding sites of Sodium atom in the Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin (pdb code 7qf7). 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 Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin, PDB code: 7qf7:

Sodium binding site 1 out of 1 in the Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Orthorhombic Crystal Structure of Ptg CBM21 in Complex with Beta- Cyclodextrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:26.6 occ:1.00 O A:LYS182 2.3 22.9 1.0 O A:HOH481 2.4 22.8 1.0 O A:HOH442 2.4 28.1 1.0 O A:HOH521 2.4 30.9 1.0 O A:HOH496 2.5 34.7 1.0 O3 C:GLC5 2.7 22.7 1.0 C A:LYS182 3.4 21.6 1.0 O A:HOH526 3.7 37.7 1.0 C3 C:GLC5 3.8 22.4 1.0 O2 C:GLC6 4.0 26.5 1.0 N A:LYS182 4.0 21.1 1.0 C4 C:GLC5 4.1 22.0 1.0 C2 C:GLC5 4.2 21.9 1.0 O A:HOH448 4.3 21.6 1.0 OE1 A:GLU181 4.3 26.8 1.0 O A:HOH520 4.3 52.9 1.0 N A:LYS183 4.3 20.9 1.0 CA A:LYS182 4.4 20.4 1.0 O A:HOH515 4.4 51.6 1.0 CA A:LYS183 4.5 20.6 1.0 O A:HOH510 4.5 34.3 1.0 O A:HOH456 4.6 34.8 1.0 O4 C:GLC5 4.6 21.7 1.0 O A:HOH528 4.6 36.8 1.0 O2 C:GLC5 4.7 21.7 1.0 O A:HOH525 4.9 43.1 1.0 C1 C:GLC6 4.9 22.2 1.0 C2 C:GLC6 5.0 24.1 1.0

M.S.Semrau, G.Giachin, S.Covaceuszach, A.Cassetta, N.Demitri, P.Storici, G.Lolli. Molecular Architecture of the Glycogen- Committed PP1/Ptg Holoenzyme. Nat Commun V. 13 6199 2022.
ISSN: ESSN 2041-1723
PubMed: 36261419
DOI: 10.1038/S41467-022-33693-Z