Calcium in PDB 6sau: Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance

The structure of Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance, PDB code: 6sau was solved by C.Roth, O.V.Moroz, J.P.Turkenburg, E.Blagova, J.Waterman, A.Ariza, L.Ming, S.Tinaqi, C.Andersen, G.J.Davies, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.13 / 1.35
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	56.877, 61.966, 70.395, 79.33, 82.88, 67.99
R / Rfree (%)	11.3 / 15

The structure of Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Calcium atom in the Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance (pdb code 6sau). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance, PDB code: 6sau:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:6.9 occ:1.00 O A:HIS214 2.4 6.6 1.0 O A:HOH713 2.4 7.8 1.0 OD1 A:ASN133 2.4 7.4 1.0 O A:GLU169 2.4 7.8 1.0 OD2 A:ASP179 2.4 9.4 1.0 O A:HOH715 2.5 7.8 1.0 O A:HOH691 2.5 9.4 1.0 OD1 A:ASP179 2.8 10.1 1.0 CG A:ASP179 3.0 8.4 1.0 C A:GLU169 3.4 6.8 1.0 CG A:ASN133 3.5 7.6 1.0 C A:HIS214 3.5 6.0 1.0 ND2 A:ASN133 4.1 7.5 1.0 CA A:GLU169 4.1 7.1 1.0 CB A:HIS214 4.2 5.0 1.0 O A:ASN133 4.3 6.9 1.0 CA A:HIS214 4.4 5.5 1.0 N A:THR170 4.4 7.5 1.0 CB A:ASP179 4.4 8.7 1.0 N A:VAL215 4.4 6.1 1.0 O A:LEU180 4.4 7.8 1.0 CG2 A:VAL215 4.5 7.0 1.0 CA A:VAL215 4.5 6.1 1.0 CE1 A:HIS155 4.5 8.7 1.0 O A:ILE168 4.6 6.8 1.0 CA A:THR170 4.6 7.8 1.0 ND1 A:HIS155 4.6 10.8 1.0 CB A:ASN133 4.7 7.1 1.0 O A:CYS171 4.7 9.3 1.0 OG1 A:THR182 4.9 8.7 1.0 CA A:ASN133 4.9 6.5 1.0 CB A:GLU169 5.0 8.0 1.0

Calcium binding site 2 out of 2 in the Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structural and Functional Characterisation of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca502 b:5.8 occ:1.00 O B:HIS214 2.4 4.8 1.0 OD1 B:ASN133 2.4 6.3 1.0 O B:HOH755 2.4 6.3 1.0 O B:HOH725 2.4 6.4 1.0 O B:GLU169 2.4 6.5 1.0 O B:HOH733 2.5 7.6 1.0 OD2 B:ASP179 2.5 7.1 1.0 OD1 B:ASP179 2.7 7.0 1.0 CG B:ASP179 2.9 6.6 1.0 C B:GLU169 3.5 6.1 1.0 CG B:ASN133 3.5 5.5 1.0 C B:HIS214 3.5 5.3 1.0 ND2 B:ASN133 4.0 6.8 1.0 CA B:GLU169 4.2 5.6 1.0 CB B:HIS214 4.3 5.3 1.0 O B:ASN133 4.4 6.3 1.0 N B:THR170 4.4 6.4 1.0 CA B:HIS214 4.4 5.0 1.0 CG2 B:VAL215 4.4 6.9 1.0 N B:VAL215 4.4 4.8 1.0 CB B:ASP179 4.4 6.4 1.0 O B:LEU180 4.5 5.8 1.0 NE2 B:HIS155 4.5 13.2 1.0 CA B:VAL215 4.5 5.4 1.0 O B:ILE168 4.6 6.0 1.0 CD2 B:HIS155 4.6 6.9 1.0 O B:CYS171 4.6 6.8 1.0 CB B:ASN133 4.7 5.3 1.0 CA B:THR170 4.7 6.7 1.0 OG1 B:THR182 4.9 8.2 1.0 CA B:ASN133 4.9 5.3 1.0

C.Roth, O.V.Moroz, J.P.Turkenburg, E.Blagova, J.Waterman, A.Ariza, L.Ming, S.Tianqi, C.Andersen, G.J.Davies, K.S.Wilson. Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance. Int J Mol Sci V. 20 2019.
ISSN: ESSN 1422-0067
PubMed: 31623309
DOI: 10.3390/IJMS20194902