Chlorine in PDB 3wwp: S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)

The structure of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2), PDB code: 3wwp 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)	45.99 / 1.90
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	191.962, 261.581, 91.987, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 19.9

The binding sites of Chlorine atom in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) (pdb code 3wwp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2), PDB code: 3wwp:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl309 b:20.8 occ:1.00 NZ A:LYS236 3.1 11.2 1.0 CD2 A:HIS235 3.3 11.1 1.0 O1 A:EDO302 3.3 47.5 1.0 O2 A:EDO302 3.4 37.9 1.0 C1 A:EDO302 3.5 49.2 1.0 NE2 A:HIS235 3.5 12.3 1.0 CG2 A:THR11 3.7 14.0 1.0 CG2 A:ILE157 3.8 13.6 1.0 CE1 A:HIS14 3.8 13.2 1.0 CE A:LYS236 3.9 12.3 1.0 OG A:SER80 3.9 15.9 1.0 C2 A:EDO302 4.0 47.9 1.0 CD1 A:ILE157 4.0 16.0 1.0 CB A:SER80 4.1 16.9 1.0 CG1 A:ILE157 4.2 14.6 1.0 NE2 A:HIS14 4.4 13.0 1.0 CD A:LYS236 4.5 13.0 1.0 ND1 A:HIS14 4.5 10.5 1.0 CB A:THR11 4.6 13.2 1.0 CB A:ILE157 4.6 15.2 1.0 CG A:HIS235 4.7 10.8 1.0 OG1 A:THR11 4.7 12.9 1.0 CE1 A:HIS235 4.8 11.5 1.0 OE1 A:GLU79 4.9 13.4 1.0

Chlorine binding site 2 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl311 b:21.8 occ:1.00 NZ B:LYS236 3.1 13.4 1.0 O2 B:EDO302 3.2 54.6 1.0 O B:HOH613 3.3 47.0 1.0 CD2 B:HIS235 3.4 16.1 1.0 C2 B:EDO302 3.5 35.7 1.0 NE2 B:HIS235 3.6 16.2 1.0 CG2 B:THR11 3.7 13.9 1.0 CG2 B:ILE157 3.7 15.0 1.0 CE B:LYS236 3.8 15.1 1.0 OG B:SER80 3.8 18.9 1.0 CD1 B:ILE157 3.9 18.4 1.0 CE1 B:HIS14 3.9 12.6 1.0 CB B:SER80 4.1 18.9 1.0 C1 B:EDO302 4.2 48.7 1.0 CG1 B:ILE157 4.3 17.7 1.0 NE2 B:HIS14 4.4 12.7 1.0 ND1 B:HIS14 4.5 12.3 1.0 CD B:LYS236 4.5 15.1 1.0 CB B:THR11 4.6 14.1 1.0 CB B:ILE157 4.7 16.3 1.0 O B:HOH786 4.7 50.7 1.0 CG B:HIS235 4.7 13.3 1.0 OG1 B:THR11 4.7 14.1 1.0 OE1 B:GLU79 4.8 15.7 1.0 CE1 B:HIS235 4.9 17.5 1.0

Chlorine binding site 3 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl307 b:30.5 occ:1.00 NZ G:LYS236 3.1 16.0 1.0 O1 G:EDO302 3.3 58.1 1.0 CD2 G:HIS235 3.4 23.9 1.0 NE2 G:HIS235 3.6 27.8 1.0 CG2 G:ILE157 3.7 25.5 1.0 CG2 G:THR11 3.7 26.4 1.0 CE G:LYS236 3.7 18.0 1.0 O2 G:EDO302 3.8 52.8 1.0 CE1 G:HIS14 3.8 21.7 1.0 C1 G:EDO302 3.9 60.2 1.0 OG G:SER80 3.9 26.0 1.0 CD1 G:ILE157 3.9 30.3 1.0 CB G:SER80 4.2 22.3 1.0 CG1 G:ILE157 4.2 27.4 1.0 C2 G:EDO302 4.4 50.6 1.0 NE2 G:HIS14 4.4 21.9 1.0 ND1 G:HIS14 4.5 20.7 1.0 CD G:LYS236 4.5 20.0 1.0 CB G:ILE157 4.6 30.3 1.0 CB G:THR11 4.7 24.1 1.0 OG1 G:THR11 4.7 23.8 1.0 CG G:HIS235 4.8 26.6 1.0 OE1 G:GLU79 4.9 25.3 1.0 CE1 G:HIS235 4.9 27.3 1.0

Chlorine binding site 4 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ L:Cl309 b:20.8 occ:1.00 NZ L:LYS236 3.1 13.1 1.0 C1 L:EDO302 3.3 30.0 1.0 CD2 L:HIS235 3.3 17.1 1.0 O L:HOH583 3.3 50.1 1.0 NE2 L:HIS235 3.5 15.7 1.0 O1 L:EDO302 3.6 50.2 1.0 CG2 L:THR11 3.6 15.3 1.0 CG2 L:ILE157 3.7 17.5 1.0 CE1 L:HIS14 3.8 18.6 1.0 CE L:LYS236 3.8 13.6 1.0 OG L:SER80 3.9 18.2 1.0 CD1 L:ILE157 4.0 17.9 1.0 CB L:SER80 4.1 17.7 1.0 C2 L:EDO302 4.2 47.6 1.0 CG1 L:ILE157 4.3 16.5 1.0 NE2 L:HIS14 4.5 17.1 1.0 ND1 L:HIS14 4.5 16.7 1.0 CD L:LYS236 4.6 14.5 1.0 CB L:THR11 4.6 14.2 1.0 CG L:HIS235 4.6 15.2 1.0 CB L:ILE157 4.6 17.6 1.0 OG1 L:THR11 4.7 16.0 1.0 OE1 L:GLU79 4.8 17.6 1.0 CE1 L:HIS235 4.9 17.6 1.0

Chlorine binding site 5 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ M:Cl305 b:36.8 occ:1.00 NZ M:LYS236 3.0 29.1 1.0 CD2 M:HIS235 3.3 32.8 1.0 NE2 M:HIS235 3.5 34.1 1.0 O1 M:EDO302 3.5 47.2 1.0 CG2 M:THR11 3.7 32.0 1.0 CE M:LYS236 3.7 27.1 1.0 CG2 M:ILE157 3.7 31.3 1.0 CE1 M:HIS14 3.8 26.0 1.0 O2 M:EDO302 3.8 55.9 1.0 OG M:SER80 3.9 32.6 1.0 CD1 M:ILE157 4.0 29.9 1.0 C2 M:EDO302 4.1 57.6 1.0 CB M:SER80 4.2 30.4 1.0 CG1 M:ILE157 4.2 31.9 1.0 C1 M:EDO302 4.2 53.2 1.0 NE2 M:HIS14 4.3 26.2 1.0 ND1 M:HIS14 4.4 27.5 1.0 CD M:LYS236 4.5 30.4 1.0 CB M:ILE157 4.6 32.9 1.0 CG M:HIS235 4.6 31.8 1.0 CB M:THR11 4.7 33.9 1.0 OG1 M:THR11 4.8 35.1 1.0 CE1 M:HIS235 4.8 36.0 1.0 OE1 M:GLU79 4.9 29.4 1.0

Chlorine binding site 6 out of 6 in the S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of S-Selective Hydroxynitrile Lyase From Baliospermum Montanum (APO2) within 5.0Å range: probe atom residue distance (Å) B Occ R:Cl308 b:26.9 occ:1.00 O2 R:EDO302 3.1 48.7 1.0 NZ R:LYS236 3.1 18.7 1.0 O R:HOH698 3.2 67.6 1.0 CD2 R:HIS235 3.4 21.0 1.0 NE2 R:HIS235 3.5 18.6 1.0 CG2 R:THR11 3.6 22.6 1.0 CG2 R:ILE157 3.7 22.8 1.0 CE1 R:HIS14 3.8 20.1 1.0 CE R:LYS236 3.8 19.3 1.0 OG R:SER80 3.9 22.3 1.0 O1 R:EDO302 4.0 52.5 1.0 CD1 R:ILE157 4.1 23.5 1.0 CB R:SER80 4.2 22.7 1.0 C2 R:EDO302 4.2 50.1 1.0 CG1 R:ILE157 4.3 19.3 1.0 NE2 R:HIS14 4.4 17.4 1.0 ND1 R:HIS14 4.4 19.1 1.0 CD R:LYS236 4.5 18.9 1.0 CB R:THR11 4.6 20.4 1.0 CB R:ILE157 4.7 21.7 1.0 CG R:HIS235 4.7 19.5 1.0 OG1 R:THR11 4.7 22.1 1.0 C1 R:EDO302 4.7 44.9 1.0 CE1 R:HIS235 4.8 19.8 1.0 OE1 R:GLU79 4.9 20.5 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