Rubidium in PDB 1hxe: Serine Protease

All present enzymatic activity of Serine Protease:
3.4.21.5;

The structure of Serine Protease, PDB code: 1hxe was solved by A.Tulinsky, E.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.500, 72.300, 73.300, 90.00, 101.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Rubidium atom in the Serine Protease (pdb code 1hxe). This binding sites where shown within 5.0 Angstroms radius around Rubidium atom.
In total 2 binding sites of Rubidium where determined in the Serine Protease, PDB code: 1hxe:
Jump to Rubidium binding site number: 1; 2;

Rubidium binding site 1 out of 2 in the Serine Protease


Mono view


Stereo pair view

A full contact list of Rubidium with other atoms in the Rb binding site number 1 of Serine Protease within 5.0Å range: probe atom residue distance (Å) B Occ H:Rb550 b:41.5 occ:0.52 O H:LYS224 2.7 32.2 1.0 O H:ARG221A 2.9 36.5 1.0 O H:HOH537 3.0 37.3 0.7 O H:HOH520 3.1 28.1 0.8 O H:HOH519 3.1 26.7 0.6 O H:HOH538 3.3 32.8 0.7 O H:HOH469 3.5 42.2 1.0 O H:TYR184A 3.6 35.5 1.0 C H:LYS224 3.9 32.7 1.0 C H:ARG221A 4.1 37.4 1.0 OD1 H:ASP222 4.5 50.0 1.0 N H:LYS224 4.5 34.5 1.0 O H:HOH539 4.5 35.2 0.9 N H:TYR184A 4.5 26.4 1.0 N H:ARG221A 4.6 37.9 1.0 CD1 H:TYR225 4.7 26.4 1.0 N H:GLY223 4.7 33.5 1.0 CA H:ASP222 4.7 37.3 1.0 C H:TYR184A 4.7 32.5 1.0 CA H:ASP221 4.8 38.5 1.0 C H:ASP221 4.8 39.3 1.0 N H:TYR225 4.8 30.6 1.0 CE1 H:TYR225 4.8 28.0 1.0 CA H:TYR225 4.8 29.4 1.0 OD1 H:ASP221 4.9 36.3 1.0 CA H:LYS224 4.9 31.7 1.0 CA H:GLY184 4.9 23.8 1.0 N H:ASP222 5.0 38.0 1.0

Rubidium binding site 2 out of 2 in the Serine Protease


Mono view


Stereo pair view

A full contact list of Rubidium with other atoms in the Rb binding site number 2 of Serine Protease within 5.0Å range: probe atom residue distance (Å) B Occ H:Rb551 b:21.4 occ:0.63 O H:HOH540 1.6 21.6 0.4 O H:THR172 2.9 27.9 1.0 O H:LYS169 2.9 30.1 1.0 O H:HOH542 3.0 22.6 0.4 O H:HOH541 3.4 23.7 0.6 C H:LYS169 3.9 26.2 1.0 C H:THR172 4.1 26.1 1.0 CA H:ASP170 4.5 26.6 1.0 N H:ASP170 4.6 26.4 1.0 CA H:ARG173 4.6 28.7 1.0 N H:ARG173 4.7 28.1 1.0 OD1 H:ASP170 4.8 22.3 1.0 CA H:LYS169 4.9 28.6 1.0 N H:THR172 5.0 25.6 1.0

E.Zhang, A.Tulinsky. The Molecular Environment of the Na+ Binding Site of Thrombin. Biophys.Chem. V. 63 185 1997.
ISSN: ISSN 0301-4622
PubMed: 9108691
DOI: 10.1016/S0301-4622(96)02227-2