Chlorine in PDB 2d0d: Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant

All present enzymatic activity of Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant:
3.7.1.9;

The structure of Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant, PDB code: 2d0d was solved by S.Y.Jun, S.Fushinobu, H.Nojiri, T.Omori, H.Shoun, T.Wakagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.84 / 1.65
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	76.650, 116.623, 78.640, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 19.1

The binding sites of Chlorine atom in the Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant (pdb code 2d0d). 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 Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant, PDB code: 2d0d:

Chlorine binding site 1 out of 1 in the Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Meta-Cleavage Product Hydrolase (Cumd) A129V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl400 b:12.1 occ:1.00 OG A:SER34 2.8 16.8 1.0 OG A:SER103 3.0 10.0 1.0 O A:HOH509 3.2 18.7 1.0 N A:SER34 3.2 10.3 1.0 N A:PHE104 3.3 6.8 1.0 CB A:PHE104 3.3 11.8 1.0 CB A:SER103 3.3 11.3 1.0 CB A:SER34 3.8 11.4 1.0 CA A:PHE104 3.9 9.2 1.0 CA A:SER34 4.0 11.6 1.0 C A:GLY33 4.1 11.4 1.0 CA A:GLY33 4.2 10.5 1.0 C A:SER103 4.3 6.8 1.0 CA A:SER103 4.4 8.8 1.0 C A:SER34 4.5 16.5 1.0 NE1 A:TRP143 4.6 8.1 1.0 CG A:PHE104 4.6 11.8 1.0 CD1 A:LEU139 4.8 10.6 1.0 CG2 A:VAL129 4.8 8.8 1.0 CZ2 A:TRP143 4.9 8.6 1.0 N A:GLY35 4.9 12.9 1.0 O A:ASN102 4.9 8.2 1.0 NE2 A:HIS252 5.0 13.7 1.0

S.Y.Jun, S.Fushinobu, H.Nojiri, T.Omori, H.Shoun, T.Wakagi. Improving the Catalytic Efficiency of A Meta-Cleavage Product Hydrolase (Cumd) From Pseudomonas Fluorescens IP01 Biochim.Biophys.Acta V.1764 1159 2006.
ISSN: ISSN 0006-3002
PubMed: 16844437
DOI: 10.1016/J.BBAPAP.2006.05.010