Calcium in PDB 6isp: Structure of Candida Antarctica Lipase B Mutant

All present enzymatic activity of Structure of Candida Antarctica Lipase B Mutant:
3.1.1.3;

The structure of Structure of Candida Antarctica Lipase B Mutant, PDB code: 6isp was solved by Y.X.Cen, J.H.Zhou, Q.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.27 / 1.88
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.980, 155.970, 92.530, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 23.8

The binding sites of Calcium atom in the Structure of Candida Antarctica Lipase B Mutant (pdb code 6isp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Candida Antarctica Lipase B Mutant, PDB code: 6isp:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Candida Antarctica Lipase B Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Candida Antarctica Lipase B Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:25.1 occ:1.00 OD2 D:ASP223 2.4 24.0 1.0 O A:HOH699 2.4 29.7 1.0 OD2 A:ASP223 2.4 23.1 1.0 O D:HOH651 2.4 24.1 1.0 O D:HOH698 2.5 23.4 1.0 O A:HOH668 2.5 25.4 1.0 O D:HOH691 2.6 25.3 1.0 CG D:ASP223 3.4 22.1 1.0 CG A:ASP223 3.5 24.8 1.0 CB D:ASP223 3.8 21.7 1.0 CB A:ASP223 4.1 24.0 1.0 O D:HOH696 4.1 27.1 1.0 O A:HOH664 4.3 30.3 1.0 O A:HOH680 4.4 31.3 1.0 OD1 D:ASP223 4.4 22.4 1.0 O D:HOH661 4.4 27.4 1.0 OD1 A:ASP223 4.5 25.8 1.0 O D:HOH656 4.6 26.4 1.0 O D:HOH578 4.6 20.2 1.0 O A:HOH537 4.7 26.6 1.0 O D:HOH645 4.9 27.6 1.0

Calcium binding site 2 out of 2 in the Structure of Candida Antarctica Lipase B Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Candida Antarctica Lipase B Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:22.0 occ:1.00 O B:HOH674 2.4 20.7 1.0 OD2 B:ASP223 2.4 22.6 1.0 OD2 C:ASP223 2.4 22.9 1.0 O B:HOH706 2.4 30.5 1.0 O C:HOH646 2.4 28.2 1.0 O B:HOH704 2.5 29.8 1.0 O C:HOH673 2.5 24.1 1.0 CG B:ASP223 3.4 21.4 1.0 CG C:ASP223 3.5 22.5 1.0 CB B:ASP223 3.9 20.6 1.0 O B:HOH687 4.0 30.7 1.0 CB C:ASP223 4.1 15.8 1.0 O C:HOH697 4.2 30.8 1.0 O B:HOH728 4.3 19.1 1.0 O B:HOH647 4.3 26.4 1.0 O B:HOH703 4.4 23.8 1.0 O B:HOH526 4.4 17.9 1.0 OD1 B:ASP223 4.4 22.1 1.0 OD1 C:ASP223 4.5 21.3 1.0 O C:HOH655 4.5 25.8 1.0 O B:HOH679 4.6 23.4 1.0 O C:HOH650 4.6 25.9 1.0 O C:HOH798 4.7 29.4 1.0 O C:HOH518 4.7 20.2 1.0 O B:HOH792 4.7 21.9 1.0 O B:HOH697 4.9 21.8 1.0 O C:HOH501 5.0 28.1 1.0 O C:HOH695 5.0 24.4 1.0

Y.Cen, W.Singh, M.Arkin, T.S.Moody, M.Huang, J.Zhou, Q.Wu, M.T.Reetz. Artificial Cysteine-Lipases with High Activity and Altered Catalytic Mechanism Created By Laboratory Evolution. Nat Commun V. 10 3198 2019.
ISSN: ESSN 2041-1723
PubMed: 31324776
DOI: 10.1038/S41467-019-11155-3