Calcium in PDB 7pth: C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline

All present enzymatic activity of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline:
3.1.6.6;

The structure of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline, PDB code: 7pth was solved by J.A.Gavira, S.Martinez-Rodriguez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.49 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.773, 103.973, 108.966, 90, 104.04, 90
R / Rfree (%)	16.3 / 20.1

The binding sites of Calcium atom in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline (pdb code 7pth). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline, PDB code: 7pth:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca602 b:31.5 occ:1.00 OD2 A:ASP296 2.3 22.2 1.0 OD1 A:ASP14 2.4 20.6 1.0 NE2 A:HIS297 2.5 20.6 1.0 OD2 A:ASP14 2.5 24.2 1.0 HB2 A:SER54 2.5 28.8 1.0 CG A:ASP14 2.7 21.6 1.0 O A:HOH1021 3.2 24.4 1.0 CG A:ASP296 3.2 21.6 1.0 HD2 A:HIS201 3.2 28.2 1.0 HZ3 A:LYS102 3.2 31.1 1.0 CB A:SER54 3.2 24.0 1.0 CD2 A:HIS297 3.3 20.9 1.0 CE1 A:HIS297 3.3 22.1 1.0 HA A:SER54 3.3 25.3 1.0 OD1 A:ASP296 3.3 20.5 1.0 OG A:SER54 3.4 24.1 1.0 HD2 A:HIS297 3.4 25.1 1.0 HE1 A:HIS297 3.5 26.6 1.0 HG A:SER54 3.5 29.0 1.0 HE A:ARG58 3.6 25.3 1.0 HZ1 A:LYS102 3.6 31.1 1.0 HH21 A:ARG58 3.6 25.2 1.0 CA A:SER54 3.8 21.0 1.0 NZ A:LYS102 3.8 25.9 1.0 HZ1 A:LYS309 4.0 26.7 1.0 CD2 A:HIS201 4.1 23.5 1.0 HB3 A:SER54 4.1 28.8 1.0 H A:GLN15 4.1 22.9 1.0 HB2 A:GLN15 4.1 23.8 1.0 CB A:ASP14 4.1 20.7 1.0 HE3 A:LYS309 4.2 27.2 1.0 ND1 A:HIS297 4.3 20.3 1.0 N A:SER54 4.3 21.5 1.0 CG A:HIS297 4.3 20.0 1.0 H A:SER54 4.3 25.8 1.0 HE2 A:LYS102 4.3 27.6 1.0 HA A:ASP14 4.3 24.7 1.0 NE A:ARG58 4.4 21.1 1.0 N A:GLN15 4.4 19.0 1.0 HZ2 A:LYS102 4.5 31.1 1.0 NH2 A:ARG58 4.5 21.0 1.0 O A:HOH837 4.5 25.6 1.0 HB2 A:ASP14 4.5 24.8 1.0 CB A:ASP296 4.6 20.3 1.0 HB2 A:ASP296 4.6 24.4 1.0 CA A:ASP14 4.7 20.6 1.0 HB3 A:ASP14 4.7 24.8 1.0 CE A:LYS102 4.7 23.0 1.0 OE1 A:GLN15 4.7 20.8 1.0 NE2 A:HIS201 4.8 22.5 1.0 C A:ASP14 4.8 20.9 1.0 NZ A:LYS309 4.8 22.2 1.0 HB3 A:ASP296 5.0 24.4 1.0 CZ A:ARG58 5.0 21.3 1.0 CB A:GLN15 5.0 19.8 1.0 CE A:LYS309 5.0 22.7 1.0 HB2 A:HIS201 5.0 25.1 1.0 HA A:GLN15 5.0 24.7 1.0

Calcium binding site 2 out of 4 in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca604 b:33.5 occ:1.00 OD2 B:ASP296 2.3 23.3 1.0 NE2 B:HIS297 2.3 24.9 1.0 OD1 B:ASP14 2.4 24.0 1.0 HB2 B:SER54 2.5 31.6 1.0 OD2 B:ASP14 2.5 26.4 1.0 CG B:ASP14 2.7 24.7 1.0 O B:HOH1059 3.0 30.7 1.0 CG B:ASP296 3.2 23.8 1.0 HD2 B:HIS201 3.2 34.4 1.0 CD2 B:HIS297 3.2 24.2 1.0 HZ3 B:LYS102 3.2 32.5 1.0 CE1 B:HIS297 3.2 24.9 1.0 CB B:SER54 3.3 26.3 1.0 HA B:SER54 3.3 27.7 1.0 OD1 B:ASP296 3.3 21.6 1.0 HD2 B:HIS297 3.3 29.1 1.0 HE1 B:HIS297 3.4 30.0 1.0 HZ1 B:LYS102 3.4 32.5 1.0 OG B:SER54 3.6 24.5 1.0 HE B:ARG58 3.6 28.0 1.0 NZ B:LYS102 3.7 27.0 1.0 CA B:SER54 3.8 23.1 1.0 HH21 B:ARG58 3.8 27.1 1.0 HZ1 B:LYS309 4.0 32.9 1.0 HB2 B:GLN15 4.0 30.0 1.0 CD2 B:HIS201 4.1 28.7 1.0 HB3 B:SER54 4.1 31.6 1.0 H B:GLN15 4.2 28.5 1.0 CB B:ASP14 4.2 24.6 1.0 HE3 B:LYS309 4.2 33.5 1.0 ND1 B:HIS297 4.2 24.2 1.0 CG B:HIS297 4.2 23.4 1.0 H B:SER54 4.3 28.0 1.0 N B:SER54 4.3 23.3 1.0 HA B:ASP14 4.3 28.4 1.0 HZ2 B:LYS102 4.3 32.5 1.0 HG B:SER54 4.4 29.5 1.0 HE2 B:LYS102 4.4 32.3 1.0 N B:GLN15 4.4 23.8 1.0 NE B:ARG58 4.5 23.3 1.0 CB B:ASP296 4.5 22.8 1.0 HB2 B:ASP14 4.6 29.5 1.0 O B:HOH750 4.6 27.1 1.0 NH2 B:ARG58 4.6 22.5 1.0 HB2 B:ASP296 4.6 27.4 1.0 CA B:ASP14 4.7 23.6 1.0 OE1 B:GLN15 4.7 26.3 1.0 CE B:LYS102 4.7 26.9 1.0 HB3 B:ASP14 4.7 29.5 1.0 NZ B:LYS309 4.8 27.4 1.0 C B:ASP14 4.8 23.7 1.0 NE2 B:HIS201 4.8 27.9 1.0 HB2 B:HIS201 4.9 31.5 1.0 CB B:GLN15 4.9 24.9 1.0 HA B:GLN15 4.9 29.3 1.0 CE B:LYS309 4.9 27.9 1.0 HB3 B:ASP296 4.9 27.4 1.0 HD1 B:HIS297 5.0 29.1 1.0

Calcium binding site 3 out of 4 in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca604 b:33.7 occ:1.00 OD2 C:ASP296 2.3 21.8 1.0 OD1 C:ASP14 2.4 23.0 1.0 NE2 C:HIS297 2.4 21.6 1.0 HB2 C:SER54 2.5 29.4 1.0 OD2 C:ASP14 2.5 22.0 1.0 CG C:ASP14 2.7 23.2 1.0 O C:HOH1116 3.0 23.8 1.0 HZ3 C:LYS102 3.0 31.8 1.0 CG C:ASP296 3.2 21.7 1.0 HD2 C:HIS201 3.2 29.4 1.0 CE1 C:HIS297 3.2 22.8 1.0 CB C:SER54 3.3 24.4 1.0 CD2 C:HIS297 3.3 22.1 1.0 OD1 C:ASP296 3.3 21.3 1.0 HA C:SER54 3.4 25.9 1.0 HE1 C:HIS297 3.4 27.4 1.0 HD2 C:HIS297 3.5 26.6 1.0 OG C:SER54 3.5 25.4 1.0 HG C:SER54 3.6 30.5 1.0 HZ1 C:LYS102 3.6 31.8 1.0 HH21 C:ARG58 3.6 27.4 1.0 NZ C:LYS102 3.7 26.4 1.0 HE C:ARG58 3.7 27.8 1.0 CA C:SER54 3.8 21.5 1.0 HZ1 C:LYS309 3.9 29.3 1.0 HB2 C:GLN15 4.0 27.3 1.0 HB3 C:SER54 4.0 29.4 1.0 H C:GLN15 4.1 25.1 1.0 CD2 C:HIS201 4.1 24.4 1.0 HE3 C:LYS309 4.1 27.0 1.0 CB C:ASP14 4.2 21.3 1.0 ND1 C:HIS297 4.2 20.9 1.0 O C:HOH1062 4.3 24.3 1.0 CG C:HIS297 4.3 20.7 1.0 HA C:ASP14 4.3 26.6 1.0 HZ2 C:LYS102 4.3 31.8 1.0 HE2 C:LYS102 4.4 29.5 1.0 N C:GLN15 4.4 20.9 1.0 N C:SER54 4.4 21.5 1.0 H C:SER54 4.5 25.9 1.0 NH2 C:ARG58 4.5 22.8 1.0 NE C:ARG58 4.5 23.1 1.0 CB C:ASP296 4.6 21.1 1.0 HB2 C:ASP14 4.6 25.6 1.0 HB2 C:ASP296 4.6 25.3 1.0 CA C:ASP14 4.6 22.2 1.0 CE C:LYS102 4.7 24.6 1.0 HB3 C:ASP14 4.7 25.6 1.0 NZ C:LYS309 4.7 24.4 1.0 OE1 C:GLN15 4.7 23.8 1.0 NE2 C:HIS201 4.8 24.3 1.0 C C:ASP14 4.8 21.3 1.0 CE C:LYS309 4.9 22.5 1.0 CB C:GLN15 4.9 22.8 1.0 HA C:GLN15 4.9 25.5 1.0 HB3 C:ASP296 5.0 25.3 1.0 HD1 C:HIS297 5.0 25.1 1.0

Calcium binding site 4 out of 4 in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Choline within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca603 b:33.7 occ:1.00 OD2 D:ASP296 2.3 20.4 1.0 OD1 D:ASP14 2.4 22.6 1.0 NE2 D:HIS297 2.4 21.2 1.0 OD2 D:ASP14 2.5 25.0 1.0 HB2 D:SER54 2.6 28.9 1.0 CG D:ASP14 2.7 23.1 1.0 HZ3 D:LYS102 3.0 30.4 1.0 CG D:ASP296 3.1 22.2 1.0 O D:HOH1045 3.1 24.3 1.0 CE1 D:HIS297 3.2 21.8 1.0 CB D:SER54 3.3 24.1 1.0 OD1 D:ASP296 3.3 21.1 1.0 HA D:SER54 3.3 25.5 1.0 CD2 D:HIS297 3.3 21.3 1.0 HD2 D:HIS201 3.3 28.9 1.0 OG D:SER54 3.4 24.1 1.0 HE1 D:HIS297 3.4 26.2 1.0 HD2 D:HIS297 3.5 25.6 1.0 HE D:ARG58 3.5 27.0 1.0 HZ1 D:LYS102 3.6 30.4 1.0 HH21 D:ARG58 3.6 28.0 1.0 NZ D:LYS102 3.7 25.3 1.0 CA D:SER54 3.7 21.2 1.0 HZ2 D:LYS309 3.9 28.4 1.0 HB2 D:GLN15 4.1 25.6 1.0 HB3 D:SER54 4.1 28.9 1.0 H D:GLN15 4.1 24.8 1.0 CB D:ASP14 4.1 21.5 1.0 HZ2 D:LYS102 4.1 30.4 1.0 HG D:SER54 4.2 29.0 1.0 CD2 D:HIS201 4.2 24.1 1.0 ND1 D:HIS297 4.3 19.9 1.0 N D:SER54 4.3 21.9 1.0 CG D:HIS297 4.3 20.4 1.0 H D:SER54 4.3 26.3 1.0 HA D:ASP14 4.3 25.9 1.0 HE3 D:LYS309 4.4 26.7 1.0 NE D:ARG58 4.4 22.4 1.0 O D:HOH922 4.4 22.6 1.0 N D:GLN15 4.4 20.6 1.0 NH2 D:ARG58 4.4 23.3 1.0 CB D:ASP296 4.5 21.7 1.0 HB2 D:ASP14 4.5 25.9 1.0 HB2 D:ASP296 4.6 26.0 1.0 NZ D:LYS309 4.6 23.7 1.0 HE2 D:LYS102 4.6 28.6 1.0 CA D:ASP14 4.7 21.5 1.0 HZ1 D:LYS309 4.7 28.4 1.0 HB3 D:ASP14 4.7 25.9 1.0 OE1 D:GLN15 4.8 23.6 1.0 CE D:LYS102 4.8 23.8 1.0 C D:ASP14 4.8 21.0 1.0 NE2 D:HIS201 4.8 25.4 1.0 HA D:GLN15 4.9 26.3 1.0 HB3 D:ASP296 4.9 26.0 1.0 CZ D:ARG58 4.9 21.8 1.0 CB D:GLN15 4.9 21.3 1.0 HD3 D:LYS102 5.0 26.2 1.0 HD1 D:HIS297 5.0 23.9 1.0

J.A.Gavira, A.Camara-Artigas, J.L.Neira, J.M.Torres De Pinedo, P.Sanchez, E.Ortega, S.Martinez-Rodriguez. Structural Insights Into Choline-O-Sulfatase Reveal the Molecular Determinants For Ligand Binding. Acta Crystallogr D Struct V. 78 669 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35503214
DOI: 10.1107/S2059798322003709