Calcium in PDB 3wwo: S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1)

The structure of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1), PDB code: 3wwo was solved by S.Nakano, M.Dadashipour, Y.Asano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.60 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.450, 68.529, 162.116, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 23.6

The binding sites of Calcium atom in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1) (pdb code 3wwo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1), PDB code: 3wwo:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:25.7 occ:1.00 NZ A:LYS236 3.1 22.7 1.0 O2 A:MPD302 3.2 26.6 1.0 CM A:MPD302 3.5 28.4 1.0 CD2 A:HIS235 3.5 20.7 1.0 CE A:LYS236 3.6 22.5 1.0 OG1 A:THR11 3.6 18.9 1.0 OG A:SER80 3.7 13.8 1.0 NE2 A:HIS235 3.7 22.3 1.0 C2 A:MPD302 3.8 26.6 1.0 CE1 A:HIS14 3.8 15.6 1.0 CG2 A:ILE157 3.9 18.4 1.0 CD1 A:ILE157 4.0 21.7 1.0 CB A:SER80 4.0 15.2 1.0 C1 A:MPD302 4.1 26.2 1.0 CG1 A:ILE157 4.3 21.3 1.0 ND1 A:HIS14 4.4 14.7 1.0 NE2 A:HIS14 4.4 14.9 1.0 CB A:THR11 4.5 15.6 1.0 CD A:LYS236 4.5 22.8 1.0 CG2 A:THR11 4.6 13.8 1.0 CB A:ILE157 4.8 21.0 1.0 CG A:HIS235 4.8 21.4 1.0

Calcium binding site 2 out of 2 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:28.8 occ:1.00 O2 B:MPD302 2.5 41.1 1.0 NZ B:LYS236 2.8 15.5 1.0 CE B:LYS236 3.3 14.0 1.0 CD2 B:HIS235 3.5 15.3 1.0 CG2 B:THR11 3.5 21.8 1.0 OG B:SER80 3.7 14.2 1.0 CE1 B:HIS14 3.7 16.2 1.0 NE2 B:HIS235 3.7 15.5 1.0 C2 B:MPD302 3.8 33.3 1.0 CG2 B:ILE157 3.8 23.5 1.0 CB B:SER80 4.0 14.1 1.0 CD1 B:ILE157 4.1 24.4 1.0 C1 B:MPD302 4.1 35.9 1.0 NE2 B:HIS14 4.2 17.6 1.0 CD B:LYS236 4.2 13.7 1.0 ND1 B:HIS14 4.3 16.4 1.0 CM B:MPD302 4.3 33.5 1.0 CG1 B:ILE157 4.4 24.4 1.0 CB B:THR11 4.6 21.4 1.0 CG B:HIS235 4.7 15.7 1.0 CB B:ILE157 4.8 23.7 1.0 OE1 B:GLU79 4.9 16.3 1.0 C3 B:MPD302 4.9 37.5 1.0 OG1 B:THR11 4.9 23.4 1.0

S.Nakano, M.Dadashipour, Y.Asano. Structural and Functional Analysis of Hydroxynitrile Lyase From Baliospermum Montanum with Crystal Structure, Molecular Dynamics and Enzyme Kinetics Biochim.Biophys.Acta V.1844 2059 2014.
ISSN: ISSN 0006-3002
PubMed: 25220808
DOI: 10.1016/J.BBAPAP.2014.09.004