Calcium in PDB 5jxg: Structure of the Unliganded Form of the Proprotein Convertase Furin.

All present enzymatic activity of Structure of the Unliganded Form of the Proprotein Convertase Furin.:
3.4.21.75;

The structure of Structure of the Unliganded Form of the Proprotein Convertase Furin., PDB code: 5jxg was solved by S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.06 / 1.80
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.957, 131.957, 155.634, 90.00, 90.00, 120.00
R / Rfree (%)	15.4 / 17.3

The structure of Structure of the Unliganded Form of the Proprotein Convertase Furin. also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	8 atoms

The binding sites of Calcium atom in the Structure of the Unliganded Form of the Proprotein Convertase Furin. (pdb code 5jxg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure of the Unliganded Form of the Proprotein Convertase Furin., PDB code: 5jxg:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Structure of the Unliganded Form of the Proprotein Convertase Furin.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Unliganded Form of the Proprotein Convertase Furin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:20.3 occ:1.00 O A:ASP181 2.3 19.5 1.0 OD2 A:ASP174 2.3 16.9 1.0 O A:HOH786 2.4 19.3 1.0 O A:HOH1187 2.4 21.7 1.0 O A:HOH751 2.5 24.8 1.0 OD1 A:ASP179 2.5 21.7 1.0 OD2 A:ASP179 2.6 24.6 1.0 CG A:ASP179 2.9 23.6 1.0 CG A:ASP174 3.3 18.9 1.0 C A:ASP181 3.5 18.3 1.0 CB A:ASP174 3.5 17.4 1.0 O A:HOH1225 4.0 40.1 1.0 CB A:ASP181 4.0 22.5 1.0 CA A:ASP181 4.2 18.7 1.0 N A:ASP181 4.4 20.1 1.0 OD1 A:ASP174 4.5 15.8 1.0 CB A:ASP179 4.5 18.8 1.0 CG A:ASP181 4.5 29.7 1.0 CB A:ASP177 4.6 19.7 1.0 N A:PRO182 4.6 18.2 1.0 OD2 A:ASP177 4.6 30.1 1.0 NH2 A:ARG225 4.6 22.9 1.0 O A:HOH1246 4.8 39.1 1.0 O A:GLN183 4.8 16.1 1.0 N A:GLN183 4.8 17.1 1.0 CA A:PRO182 4.9 19.8 1.0 OD2 A:ASP181 4.9 30.3 1.0 O A:HOH876 5.0 35.3 1.0

Calcium binding site 2 out of 3 in the Structure of the Unliganded Form of the Proprotein Convertase Furin.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Unliganded Form of the Proprotein Convertase Furin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca602 b:19.5 occ:1.00 O A:VAL210 2.3 19.0 1.0 O A:VAL205 2.4 19.0 1.0 OD2 A:ASP115 2.4 20.8 1.0 OD1 A:ASP162 2.4 21.9 1.0 O A:GLY212 2.4 17.7 1.0 OD1 A:ASN208 2.5 20.6 1.0 OD2 A:ASP162 2.6 19.0 1.0 CG A:ASP162 2.8 20.6 1.0 C A:VAL210 3.5 24.0 1.0 CG A:ASP115 3.5 17.8 1.0 C A:VAL205 3.5 20.9 1.0 CG A:ASN208 3.5 22.7 1.0 C A:GLY212 3.6 18.4 1.0 ND2 A:ASN208 3.9 18.0 1.0 N A:GLY212 4.2 19.8 1.0 CB A:ASP115 4.2 19.8 1.0 CA A:VAL210 4.2 22.3 1.0 N A:VAL210 4.2 19.3 1.0 CB A:VAL210 4.3 21.9 1.0 C A:CYS211 4.3 22.0 1.0 CB A:ASP162 4.4 18.6 1.0 CA A:ALA206 4.4 16.7 1.0 N A:ALA206 4.4 18.4 1.0 CA A:GLY212 4.4 15.9 1.0 CA A:VAL205 4.4 16.9 1.0 N A:VAL205 4.5 17.9 1.0 OD1 A:ASP115 4.5 20.1 1.0 N A:CYS211 4.5 18.1 1.0 N A:VAL213 4.6 19.1 1.0 O A:CYS211 4.7 19.7 1.0 O A:HOH957 4.7 17.7 1.0 CG1 A:VAL213 4.7 17.9 1.0 CA A:VAL213 4.7 15.2 1.0 CB A:VAL205 4.8 23.8 1.0 CA A:CYS211 4.8 18.9 1.0 C A:ALA206 4.8 23.1 1.0 N A:ASN208 4.8 23.1 1.0 CB A:CYS211 4.8 23.3 1.0 CB A:ASN208 4.8 22.7 1.0 CG1 A:VAL210 4.9 20.2 1.0 N A:ASN207 4.9 24.5 1.0 C A:ALA204 4.9 14.7 1.0

Calcium binding site 3 out of 3 in the Structure of the Unliganded Form of the Proprotein Convertase Furin.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of the Unliganded Form of the Proprotein Convertase Furin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca603 b:12.8 occ:1.00 OD1 A:ASP258 2.4 13.8 1.0 OD2 A:ASP301 2.4 12.9 1.0 O A:HOH838 2.4 10.6 1.0 OE1 A:GLU331 2.4 12.3 1.0 O A:HOH991 2.5 12.9 1.0 OE2 A:GLU331 2.5 12.8 1.0 O A:HOH1110 2.5 11.4 1.0 CD A:GLU331 2.8 11.7 1.0 CG A:ASP301 3.3 13.8 1.0 CG A:ASP258 3.4 15.7 1.0 OD1 A:ASP301 3.9 14.0 1.0 CB A:ASP258 4.1 17.5 1.0 CB A:ASP301 4.1 11.7 1.0 CA A:ASP258 4.1 14.4 1.0 OD2 A:ASP258 4.3 16.1 1.0 CG A:GLU331 4.3 12.7 1.0 O A:HOH873 4.3 14.2 1.0 CB A:ASP306 4.4 10.5 1.0 O A:HOH979 4.5 12.2 1.0 OD2 A:ASP306 4.5 13.6 1.0 CA A:GLY294 4.6 12.6 1.0 O A:HOH853 4.6 18.3 1.0 O A:SER293 4.6 14.9 1.0 CA A:CYS303 4.7 11.3 1.0 O A:GLU257 4.9 14.9 1.0 O A:PRO256 4.9 12.9 1.0 N A:GLY296 4.9 13.2 1.0 N A:ASP258 4.9 15.0 1.0 CB A:CYS303 4.9 15.1 1.0

S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than. Structure of the Unliganded Form of the Proprotein Convertase Furin Suggests Activation By A Substrate-Induced Mechanism. Proc.Natl.Acad.Sci.Usa V. 113 11196 2016.
ISSN: ESSN 1091-6490
PubMed: 27647913
DOI: 10.1073/PNAS.1613630113