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

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

The structure of C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Hepes, PDB code: 7ptj 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)	75.25 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.521, 207.007, 116.833, 90, 110.29, 90
R / Rfree (%)	16.2 / 20

The binding sites of Calcium atom in the C54S Mutant of Choline-Sulfatase From E. Meliloti CECT4857 Bound to Hepes (pdb code 7ptj). 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 Hepes, PDB code: 7ptj:
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 Hepes


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 Hepes within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1110 b:46.1 occ:0.64 OG A:SER54 2.6 21.3 1.0 OD2 A:ASP14 2.6 25.1 1.0 OD1 A:ASP14 2.8 19.1 1.0 CB A:SER54 2.8 24.3 1.0 OD2 A:ASP296 3.0 23.2 1.0 CG A:ASP14 3.1 23.2 1.0 NE2 A:HIS297 3.2 23.2 1.0 O2S A:EPE1101 3.5 27.2 0.9 CD2 A:HIS201 3.7 24.1 1.0 CA A:SER54 3.7 22.9 1.0 NZ A:LYS102 4.0 36.5 1.0 NE2 A:HIS201 4.1 27.6 1.0 CG A:ASP296 4.1 22.6 1.0 CE1 A:HIS297 4.1 23.1 1.0 CD2 A:HIS297 4.2 20.1 1.0 CE2 A:TYR123 4.3 32.8 1.0 NE A:ARG58 4.3 20.8 1.0 S A:EPE1101 4.4 36.5 0.9 O3S A:EPE1101 4.5 28.5 0.9 CE A:LYS102 4.5 28.5 1.0 OD1 A:ASP296 4.5 20.6 1.0 N A:SER54 4.5 21.8 1.0 O1S A:EPE1101 4.5 35.6 0.9 CB A:ASP14 4.6 20.2 1.0 NH2 A:ARG58 4.8 21.2 1.0 CG A:HIS201 4.9 26.7 1.0 C A:SER54 4.9 20.4 1.0 OH A:TYR123 4.9 43.6 1.0 ND1 A:HIS104 4.9 24.4 1.0 NZ A:LYS309 4.9 25.0 1.0

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


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 Hepes within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca611 b:46.3 occ:0.64 OG B:SER54 2.4 29.1 1.0 CB B:SER54 2.6 24.0 1.0 NZ B:LYS102 2.6 28.5 0.3 OD2 B:ASP14 2.8 30.2 1.0 OD1 B:ASP14 3.1 27.2 1.0 OD2 B:ASP296 3.2 23.4 1.0 O2S B:EPE602 3.2 27.8 0.7 CE1 B:HIS297 3.3 22.0 1.0 CG B:ASP14 3.3 26.4 1.0 CA B:SER54 3.6 23.0 1.0 CD2 B:HIS201 3.8 24.8 1.0 CE B:LYS102 3.9 26.2 0.3 NE2 B:HIS297 4.0 25.8 1.0 CE2 B:TYR123 4.0 36.7 1.0 S B:EPE602 4.1 39.7 0.7 O1S B:EPE602 4.2 26.8 0.7 NE2 B:HIS201 4.2 31.1 1.0 N B:SER54 4.2 21.4 1.0 NZ B:LYS102 4.2 29.7 0.7 O3S B:EPE602 4.3 37.4 0.7 NE B:ARG58 4.4 21.1 1.0 ND1 B:HIS297 4.4 23.7 1.0 CG B:ASP296 4.4 26.4 1.0 CE B:LYS102 4.7 25.3 0.7 OH B:TYR123 4.7 41.3 1.0 ND1 B:HIS104 4.8 28.9 1.0 CB B:ASP14 4.8 23.0 1.0 NH2 B:ARG58 4.8 20.0 1.0 C B:SER54 4.9 20.8 1.0 CD2 B:TYR123 4.9 31.9 1.0 OD1 B:ASP296 4.9 20.1 1.0 CZ B:TYR123 4.9 39.4 1.0 NZ B:LYS309 5.0 26.8 1.0 CG B:HIS201 5.0 29.6 1.0 CD B:LYS102 5.0 25.6 0.3

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


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 Hepes within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca614 b:56.5 occ:0.47 OD1 C:ASP14 2.3 25.1 1.0 OD2 C:ASP296 2.4 22.2 1.0 NE2 C:HIS297 2.5 26.9 1.0 OD2 C:ASP14 2.7 34.4 1.0 CG C:ASP14 2.9 29.4 1.0 CB C:SER54 2.9 23.9 0.3 OG C:SER54 3.0 23.7 0.7 CB C:SER54 3.0 23.2 0.7 CE1 C:HIS297 3.4 22.1 1.0 CD2 C:HIS297 3.4 22.6 1.0 CG C:ASP296 3.5 22.4 1.0 O2S C:EPE601 3.5 28.2 0.8 CA C:SER54 3.6 22.8 0.3 CA C:SER54 3.6 23.1 0.7 OD1 C:ASP296 3.8 23.0 1.0 CD2 C:HIS201 3.8 26.7 1.0 OG C:SER54 3.9 26.2 0.3 NZ C:LYS102 4.1 28.6 0.4 N C:SER54 4.2 22.9 0.3 NE C:ARG58 4.2 19.4 1.0 CB C:ASP14 4.3 23.8 1.0 N C:SER54 4.4 22.2 0.7 NE2 C:HIS201 4.4 29.7 1.0 NH2 C:ARG58 4.4 25.9 1.0 ND1 C:HIS297 4.5 20.4 1.0 CG C:HIS297 4.5 20.3 1.0 S C:EPE601 4.6 31.0 0.8 NZ C:LYS102 4.6 30.5 0.6 O1S C:EPE601 4.6 30.1 0.8 N C:GLN15 4.8 19.1 1.0 CB C:ASP296 4.8 19.7 1.0 CZ C:ARG58 4.8 26.1 1.0 C C:SER54 4.8 19.9 0.7 NZ C:LYS309 4.9 19.5 1.0 OE1 C:GLN15 4.9 20.6 1.0 CA C:ASP14 4.9 19.5 1.0 C C:SER54 4.9 20.1 0.3 CE2 C:TYR123 4.9 48.3 1.0 O3S C:EPE601 4.9 35.4 0.8 CG C:HIS201 5.0 27.4 1.0

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


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 Hepes within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca604 b:48.8 occ:0.55 OD1 D:ASP14 2.4 29.5 1.0 OD2 D:ASP14 2.6 38.1 1.0 OD2 D:ASP296 2.7 30.8 1.0 CG D:ASP14 2.8 29.3 1.0 CB D:SER54 3.1 32.5 0.9 CB D:SER54 3.1 32.5 0.1 NE2 D:HIS297 3.1 31.5 1.0 OG D:SER54 3.3 35.1 0.9 O3S D:EPE601 3.7 30.3 0.8 CD2 D:HIS201 3.7 32.1 1.0 CA D:SER54 3.8 28.3 0.9 CA D:SER54 3.8 28.6 0.1 CG D:ASP296 3.9 28.7 1.0 CE1 D:HIS297 4.0 29.4 1.0 CD2 D:HIS297 4.0 26.4 1.0 OG D:SER54 4.1 33.2 0.1 NZ D:LYS102 4.1 42.4 1.0 NE D:ARG58 4.2 29.5 1.0 CE2 D:TYR123 4.3 50.4 1.0 NE2 D:HIS201 4.3 32.2 1.0 CB D:ASP14 4.3 29.8 1.0 OD1 D:ASP296 4.4 26.1 1.0 NH2 D:ARG58 4.5 28.3 1.0 N D:SER54 4.6 29.0 1.0 OH D:TYR123 4.7 53.2 1.0 CE D:LYS102 4.7 40.6 1.0 O1S D:EPE601 4.7 32.9 0.8 S D:EPE601 4.7 45.2 0.8 CZ D:ARG58 4.8 34.1 1.0 CG D:HIS201 4.8 32.0 1.0 NZ D:LYS309 4.9 28.6 1.0 C D:SER54 5.0 28.0 1.0 CZ D:TYR123 5.0 55.5 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