Sodium in PDB 6sac: N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment

All present enzymatic activity of N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment:
4.2.1.1;

The structure of N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment, PDB code: 6sac was solved by S.Gloeckner, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.95 / 1.02
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.374, 41.286, 72.281, 90.00, 104.82, 90.00
R / Rfree (%)	12.6 / 14.2

The structure of N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment also contains other interesting chemical elements:

Mercury	(Hg)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Sodium atom in the N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment (pdb code 6sac). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment, PDB code: 6sac:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:20.9 occ:0.66 O A:PRO83 2.3 12.7 1.0 O A:HOH519 2.4 22.5 0.7 O1 A:PG4307 2.4 17.8 0.7 O3 A:PG4307 2.4 18.1 0.7 O4 A:PG4307 2.5 20.3 0.7 O2 A:PG4307 2.6 16.5 0.7 O5 A:PG4307 2.7 22.2 0.7 C1 A:PG4307 3.2 17.3 0.7 C5 A:PG4307 3.2 19.1 0.7 C6 A:PG4307 3.3 19.8 0.7 C4 A:PG4307 3.3 17.9 0.7 C2 A:PG4307 3.3 16.8 0.7 C7 A:PG4307 3.4 21.0 0.7 C A:PRO83 3.4 10.9 1.0 C3 A:PG4307 3.4 17.3 0.7 C8 A:PG4307 3.5 21.6 0.7 HA A:PRO83 3.7 14.1 1.0 HB2 A:PRO83 3.8 15.1 1.0 CA A:PRO83 4.0 11.7 1.0 CB A:PRO83 4.4 12.6 1.0 N A:LEU84 4.5 9.6 0.6 N A:LEU84 4.5 10.2 0.4 HA A:LEU84 4.5 10.9 0.6 HA A:LEU84 4.5 11.9 0.4 HB3 A:ASP85 4.6 16.4 0.6 HB3 A:PRO83 4.7 15.1 1.0 CA A:LEU84 4.9 9.1 0.6 C A:LEU84 4.9 10.0 0.6 CA A:LEU84 4.9 9.9 0.4

Sodium binding site 2 out of 2 in the N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of N-Terminal Expression Tag Remainder of Human Carbonic Anhydrase II Covalently Modified By Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Na302 b:17.6 occ:0.59 O A:HOH501 2.3 21.0 0.6 O A:ASP162 2.4 11.6 0.6 OD1 A:ASP165 2.4 17.9 0.6 O A:HOH424 2.5 21.1 0.6 O A:ASP162 2.5 12.3 0.4 O A:HOH556 2.6 20.8 0.6 HB2 A:ASP165 3.0 18.7 0.4 CG A:ASP165 3.1 17.7 0.6 HB2 A:ASP165 3.2 20.0 0.6 C A:ASP162 3.6 11.3 0.6 C A:ASP162 3.6 11.8 0.4 OD2 A:ASP165 3.7 18.4 0.4 CB A:ASP165 3.7 16.7 0.6 HA A:ASP162 3.9 14.4 0.4 OD2 A:ASP165 3.9 18.5 0.6 H A:ASP165 3.9 15.2 0.4 HA A:ASP162 3.9 13.8 0.6 H A:ASP165 3.9 16.0 0.6 CB A:ASP165 4.0 15.6 0.4 OD2 A:ASP162 4.1 13.4 0.6 CG A:ASP162 4.1 13.1 0.6 HB3 A:ASP162 4.1 15.9 0.4 OD1 A:ASP162 4.1 13.5 0.6 HA A:VAL163 4.2 12.5 1.0 CA A:ASP162 4.2 12.0 0.4 CG A:ASP165 4.3 17.5 0.4 CA A:ASP162 4.3 11.5 0.6 HB3 A:ASP165 4.3 20.0 0.6 HB3 A:ASP165 4.4 18.7 0.4 N A:VAL163 4.6 10.5 1.0 N A:ASP165 4.6 13.4 0.6 CB A:ASP162 4.7 13.2 0.4 N A:ASP165 4.7 12.7 0.4 O A:HOH430 4.7 39.2 1.0 CA A:VAL163 4.8 10.4 1.0 CB A:ASP162 4.8 12.4 0.6 CA A:ASP165 4.8 14.9 0.6 CA A:ASP165 4.9 13.6 0.4 OD1 A:ASP162 5.0 14.6 0.4 C A:VAL163 5.0 10.0 1.0

S.Glockner, A.Heine, G.Klebe. A Proof-of-Concept Fragment Screening of A Hit-Validated 96-Compounds Library Against Human Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32235320
DOI: 10.3390/BIOM10040518