Chlorine in PDB 4yas: Hydroxynitrile Lyase Complexed with Chloralhydrate

All present enzymatic activity of Hydroxynitrile Lyase Complexed with Chloralhydrate:
4.1.2.39;

The structure of Hydroxynitrile Lyase Complexed with Chloralhydrate, PDB code: 4yas was solved by J.Zuegg, U.G.Wagner, M.Gugganig, C.Kratky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	47.593, 106.767, 128.203, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 22.1

The binding sites of Chlorine atom in the Hydroxynitrile Lyase Complexed with Chloralhydrate (pdb code 4yas). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Hydroxynitrile Lyase Complexed with Chloralhydrate, PDB code: 4yas:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Hydroxynitrile Lyase Complexed with Chloralhydrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hydroxynitrile Lyase Complexed with Chloralhydrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl300 b:23.3 occ:1.00 CL1 A:CLX300 0.0 23.3 1.0 C1 A:CLX300 1.8 20.4 1.0 C A:CLX300 2.8 16.6 1.0 CL2 A:CLX300 2.9 24.3 1.0 CL3 A:CLX300 3.0 21.9 1.0 OG A:SER80 3.0 12.7 1.0 SG A:CYS81 3.2 17.8 1.0 CE1 A:PHE210 3.7 4.1 1.0 CZ A:PHE210 3.8 2.0 1.0 O A:CLX300 4.1 18.7 1.0 CD2 A:LEU121 4.1 9.7 1.0 CH2 A:TRP128 4.1 13.5 1.0 N A:CYS81 4.4 4.0 1.0 CB A:SER80 4.4 4.3 1.0 OG1 A:THR11 4.6 7.6 1.0 CB A:CYS81 4.8 7.9 1.0 CZ3 A:TRP128 4.8 13.6 1.0 C A:SER80 4.9 3.8 1.0 CD1 A:PHE210 5.0 2.5 1.0 CA A:CYS81 5.0 4.3 1.0

Chlorine binding site 2 out of 3 in the Hydroxynitrile Lyase Complexed with Chloralhydrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hydroxynitrile Lyase Complexed with Chloralhydrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl300 b:24.3 occ:1.00 CL2 A:CLX300 0.0 24.3 1.0 C1 A:CLX300 1.8 20.4 1.0 C A:CLX300 2.7 16.6 1.0 CL1 A:CLX300 2.9 23.3 1.0 CL3 A:CLX300 2.9 21.9 1.0 O A:CLX300 3.3 18.7 1.0 CD1 A:ILE209 3.5 2.8 1.0 CH2 A:TRP128 3.7 13.5 1.0 CZ3 A:TRP128 3.9 13.6 1.0 OG A:SER80 4.0 12.7 1.0 CE1 A:PHE210 4.1 4.1 1.0 CG1 A:ILE209 4.2 2.2 1.0 CD2 A:LEU157 4.4 2.5 1.0 CG2 A:ILE209 4.6 2.0 1.0 CZ2 A:TRP128 4.6 14.2 1.0 NE2 A:HIS235 4.7 3.3 1.0 CG A:LEU157 4.7 2.8 1.0 CD1 A:LEU157 4.7 2.5 1.0 CD1 A:PHE210 4.8 2.5 1.0 CE3 A:TRP128 4.9 12.0 1.0 CZ A:PHE210 5.0 2.0 1.0 CB A:ILE209 5.0 2.0 1.0

Chlorine binding site 3 out of 3 in the Hydroxynitrile Lyase Complexed with Chloralhydrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Hydroxynitrile Lyase Complexed with Chloralhydrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl300 b:21.9 occ:1.00 CL3 A:CLX300 0.0 21.9 1.0 C1 A:CLX300 1.8 20.4 1.0 C A:CLX300 2.8 16.6 1.0 CL2 A:CLX300 2.9 24.3 1.0 O A:CLX300 3.0 18.7 1.0 CL1 A:CLX300 3.0 23.3 1.0 OG1 A:THR11 3.5 7.6 1.0 OG A:SER80 3.5 12.7 1.0 CG1 A:ILE12 3.6 4.6 1.0 CG2 A:THR11 4.0 3.0 1.0 O A:ILE12 4.1 2.4 1.0 SG A:CYS81 4.2 17.8 1.0 CD1 A:ILE12 4.3 5.6 1.0 CB A:THR11 4.4 4.2 1.0 CD1 A:LEU148 4.6 5.0 1.0 CB A:SER80 4.6 4.3 1.0 N A:ILE12 4.6 2.0 1.0 CD2 A:LEU157 4.8 2.5 1.0 CZ3 A:TRP128 4.9 13.6 1.0 C A:ILE12 4.9 2.0 1.0 CD2 A:LEU148 4.9 5.4 1.0 CB A:ILE12 4.9 3.8 1.0 CH2 A:TRP128 5.0 13.5 1.0

J.Zuegg, K.Gruber, M.Gugganig, U.G.Wagner, C.Kratky. Three-Dimensional Structures of Enzyme-Substrate Complexes of the Hydroxynitrile Lyase From Hevea Brasiliensis. Protein Sci. V. 8 1990 1999.
ISSN: ISSN 0961-8368
PubMed: 10548044
DOI: 10.1110/PS.8.10.1990