Calcium in PDB 9h8i: Crystallization of B. Licheniformis Levanase

The structure of Crystallization of B. Licheniformis Levanase, PDB code: 9h8i was solved by S.Carr, A.Cruz-Migoni, J.R.Porras-Dominguez, W.Van Den Ende, A.Lopez-Munguia Canales, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.38 / 1.54
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.586, 82.586, 171.088, 90, 90, 90
R / Rfree (%)	19.3 / 21.7

The binding sites of Calcium atom in the Crystallization of B. Licheniformis Levanase (pdb code 9h8i). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystallization of B. Licheniformis Levanase, PDB code: 9h8i:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystallization of B. Licheniformis Levanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystallization of B. Licheniformis Levanase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:11.4 occ:1.00 OD1 A:ASN230 2.2 13.8 1.0 O4 A:BCN503 2.4 12.3 1.0 O21 A:BCN503 2.4 11.4 1.0 O21 A:BCN504 2.4 11.2 1.0 O6 A:BCN503 2.4 14.0 1.0 O A:HOH631 2.5 13.0 1.0 N1 A:BCN503 2.6 11.3 1.0 C2 A:BCN503 3.2 10.3 1.0 C4 A:BCN503 3.2 12.9 1.0 C1 A:BCN503 3.3 10.3 1.0 C3 A:BCN503 3.3 12.8 1.0 C6 A:BCN503 3.3 12.6 1.0 C2 A:BCN504 3.4 11.8 1.0 C5 A:BCN503 3.4 11.9 1.0 CG A:ASN230 3.4 13.5 1.0 O22 A:BCN504 3.7 12.6 1.0 CA A:CA502 3.9 11.9 1.0 OD2 A:ASP288 4.0 13.7 1.0 ND2 A:ASN230 4.2 11.9 1.0 O6 A:BCN504 4.2 11.8 1.0 O22 A:BCN503 4.4 11.0 1.0 O A:HOH684 4.5 11.7 1.0 CB A:ASN230 4.5 12.2 1.0 O A:PHE258 4.6 11.2 1.0 O A:HOH677 4.7 18.1 1.0 C1 A:BCN504 4.8 12.4 1.0 C6 A:BCN504 5.0 12.7 1.0 O A:ASN230 5.0 11.1 1.0

Calcium binding site 2 out of 2 in the Crystallization of B. Licheniformis Levanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystallization of B. Licheniformis Levanase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:11.9 occ:1.00 O21 A:BCN503 2.4 11.4 1.0 O4 A:BCN504 2.5 12.6 1.0 O21 A:BCN504 2.5 11.2 1.0 OD2 A:ASP288 2.5 13.7 1.0 O A:HOH780 2.5 12.8 1.0 O6 A:BCN504 2.5 11.8 1.0 N1 A:BCN504 2.6 12.3 1.0 C5 A:BCN504 3.3 12.3 1.0 C4 A:BCN504 3.3 15.3 1.0 C6 A:BCN504 3.4 12.7 1.0 C2 A:BCN503 3.4 10.3 1.0 C2 A:BCN504 3.4 11.8 1.0 C3 A:BCN504 3.4 13.8 1.0 C1 A:BCN504 3.5 12.4 1.0 CG A:ASP288 3.5 14.6 1.0 O22 A:BCN503 3.8 11.0 1.0 OD1 A:ASP288 3.9 14.1 1.0 CA A:CA501 3.9 11.4 1.0 O4 A:BCN503 4.0 12.3 1.0 O22 A:BCN504 4.6 12.6 1.0 C1 A:BCN503 4.7 10.3 1.0 OD1 A:ASN230 4.7 13.8 1.0 C3 A:BCN503 4.7 12.8 1.0 O A:HOH671 4.7 31.8 1.0 ND2 A:ASN222 4.8 12.4 1.0 CB A:ASP288 4.8 13.7 1.0 N1 A:BCN503 4.8 11.3 1.0 C4 A:BCN503 4.8 12.9 1.0

J.R.Porras-Dominguez, A.Cruz-Migoni, S.B.Carr, M.E.Rodriguez-Alegria, A.Lopez-Munguia, W.Van Den Ende. Understanding the Endo- and Exo-Mechanisms Involved in the Enzymatic Hydrolysis of Levan and Inulin Polymers. J.Agric.Food Chem. 2025.
ISSN: ESSN 1520-5118
PubMed: 40227403
DOI: 10.1021/ACS.JAFC.5C00187