Calcium in PDB 9f17: Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori

All present enzymatic activity of Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori:
6.3.4.4;

The structure of Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori, PDB code: 9f17 was solved by Z.Stefanic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.42 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.15, 122.7, 70.15, 90, 113.36, 90
R / Rfree (%)	17.8 / 21

The binding sites of Calcium atom in the Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori (pdb code 9f17). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori, PDB code: 9f17:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:24.3 occ:1.00 O1A A:GDP502 2.3 22.6 1.0 OD1 A:ASP12 2.3 21.9 1.0 O1B A:GDP502 2.3 22.4 1.0 O2 A:SO4504 2.3 23.6 1.0 O4 A:SO4505 2.3 21.8 0.7 O A:GLY39 2.4 24.7 1.0 O4 A:SO4504 3.2 23.8 1.0 S A:SO4504 3.4 22.2 1.0 CG A:ASP12 3.4 23.2 1.0 PA A:GDP502 3.5 23.9 1.0 C A:GLY39 3.5 24.5 1.0 PB A:GDP502 3.6 22.6 1.0 S A:SO4505 3.7 33.6 0.7 O3A A:GDP502 3.7 22.1 1.0 CA A:ASP12 3.8 20.6 1.0 N A:GLY39 3.9 21.6 1.0 O2 A:SO4505 4.0 41.5 0.7 CB A:ASP12 4.0 23.5 1.0 N A:ASP12 4.1 22.0 1.0 CA A:GLY39 4.1 22.6 1.0 N1 A:IMP503 4.1 27.6 1.0 O6 A:IMP503 4.2 29.9 1.0 O A:HOH837 4.2 38.9 1.0 CD2 A:HIS40 4.3 23.1 1.0 O2A A:GDP502 4.3 24.8 1.0 O1 A:SO4504 4.3 22.4 1.0 O3 A:SO4504 4.3 25.9 1.0 O A:HOH628 4.4 35.5 1.0 OD2 A:ASP12 4.5 24.7 1.0 C6 A:IMP503 4.5 30.3 1.0 O3 A:SO4505 4.5 31.8 0.7 O3B A:GDP502 4.5 22.4 1.0 O2B A:GDP502 4.5 21.6 1.0 N A:HIS40 4.6 23.5 1.0 O1 A:SO4505 4.6 39.0 0.7 O5' A:GDP502 4.7 24.8 1.0 CA A:HIS40 4.9 21.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of N Term His-Tag Adenylosuccinate Synthetase From Helicobacter Pylori within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca501 b:23.9 occ:1.00 O1A B:GDP503 2.2 25.3 1.0 O1B B:GDP503 2.3 23.0 1.0 O4 B:SO4504 2.3 22.7 0.7 O1 B:SO4505 2.3 24.9 1.0 OD1 B:ASP12 2.4 25.3 1.0 O B:GLY39 2.5 25.2 1.0 O3 B:SO4505 3.2 25.8 1.0 S B:SO4505 3.3 22.6 1.0 PA B:GDP503 3.4 25.8 1.0 CG B:ASP12 3.5 25.2 1.0 PB B:GDP503 3.5 26.1 1.0 C B:GLY39 3.5 24.3 1.0 S B:SO4504 3.7 32.7 0.7 O3A B:GDP503 3.8 23.8 1.0 CA B:ASP12 3.8 23.5 1.0 N B:GLY39 3.9 21.8 1.0 O3 B:SO4504 3.9 41.4 0.7 N B:ASP12 4.0 20.1 1.0 CB B:ASP12 4.0 23.0 1.0 CA B:GLY39 4.1 22.1 1.0 O B:HOH737 4.1 35.0 1.0 O6 B:IMP502 4.1 30.8 1.0 O2A B:GDP503 4.2 25.4 1.0 N1 B:IMP502 4.2 27.0 1.0 O4 B:SO4505 4.3 24.4 1.0 O B:HOH625 4.3 43.4 1.0 O2 B:SO4505 4.3 24.6 1.0 O B:HOH605 4.4 35.1 1.0 CD2 B:HIS40 4.4 24.1 1.0 O2 B:SO4504 4.4 34.8 0.7 O3B B:GDP503 4.5 26.4 1.0 O2B B:GDP503 4.5 23.3 1.0 C6 B:IMP502 4.5 29.2 1.0 OD2 B:ASP12 4.6 25.6 1.0 N B:HIS40 4.6 22.5 1.0 O1 B:SO4504 4.6 39.6 0.7 O5' B:GDP503 4.7 27.4 1.0 CA B:HIS40 4.9 22.6 1.0

M.Z.Miskovic, M.Wojtys, M.Winiewska-Szajewska, B.Wielgus-Kutrowska, M.Matkovic, D.Domazet Jurasin, Z.Stefanic, A.Bzowska, I.Lescic Asler. Location Is Everything: Influence of His-Tag Fusion Site on Properties of Adenylosuccinate Synthetase From Helicobacter Pylori. Int J Mol Sci V. 25 2024.
ISSN: ESSN 1422-0067
PubMed: 39062851
DOI: 10.3390/IJMS25147613