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Chlorine in PDB 3dqz: Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana

Protein crystallography data

The structure of Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana, PDB code: 3dqz was solved by J.Andexer, N.Staunig, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.17 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.248, 223.313, 50.201, 90.00, 101.47, 90.00
R / Rfree (%) 15.9 / 21

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana (pdb code 3dqz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana, PDB code: 3dqz:

Chlorine binding site 1 out of 1 in 3dqz

Go back to Chlorine Binding Sites List in 3dqz
Chlorine binding site 1 out of 1 in the Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Hydroxynitrile Lyase From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl259

b:16.4
occ:1.00
N D:GLN176 3.0 18.3 1.0
CA D:ARG175 3.4 17.2 1.0
CB D:ARG175 3.6 17.0 1.0
C D:ARG175 3.7 19.6 1.0
CB D:GLN176 3.9 21.4 1.0
CA D:GLN176 4.0 20.2 1.0
CG D:ARG175 4.2 15.0 1.0
O D:HOH268 4.3 14.1 1.0
NE D:ARG175 4.5 22.9 1.0
CE D:LYS148 4.7 15.5 1.0
O D:GLN176 4.7 19.3 1.0
O D:HIS174 4.8 19.2 1.0
N D:ARG175 4.8 18.4 1.0
C D:GLN176 4.9 20.3 1.0
CD D:LYS148 4.9 22.4 1.0
NZ D:LYS148 4.9 15.8 1.0
O D:ARG175 4.9 15.2 1.0
CD D:ARG175 4.9 18.4 1.0

Reference:

J.N.Andexer, N.Staunig, T.Eggert, C.Kratky, M.Pohl, K.Gruber. Hydroxynitrile Lyases with Alpha / Beta-Hydrolase Fold: Two Enzymes with Almost Identical 3D Structures But Opposite Enantioselectivities and Different Reaction Mechanisms Chembiochem V. 13 1932 2012.
ISSN: ISSN 1439-4227
PubMed: 22851196
DOI: 10.1002/CBIC.201200239
Page generated: Fri Jul 11 04:37:17 2025

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