Chlorine in PDB 5t79: X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol

The structure of X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol, PDB code: 5t79 was solved by J.S.Brunzelle, Z.Wawrzak, E.Evdokimova, M.Kudritska, A.Savchenko, A.F.Yakunin, W.F.Anderson, Center For Structural Genomics Ofinfectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.85 / 1.86
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	94.387, 94.387, 91.677, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.3

The binding sites of Chlorine atom in the X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol (pdb code 5t79). 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 X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol, PDB code: 5t79:

Chlorine binding site 1 out of 1 in the X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Crystal Structure of A Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:22.9 occ:1.00 O A:HOH783 3.1 28.1 1.0 NE A:ARG89 3.1 13.8 1.0 N A:GLU130 3.2 13.5 0.4 N A:GLU130 3.3 13.3 0.6 N A:TYR131 3.6 12.7 1.0 O A:HOH879 3.7 31.7 1.0 O A:TYR131 3.7 13.4 1.0 CB A:GLU130 3.8 15.1 0.4 CB A:GLU130 3.8 14.6 0.6 CD2 A:LEU129 3.8 16.4 1.0 CD A:ARG89 3.8 18.5 1.0 CA A:GLU130 3.9 13.1 0.4 CA A:GLU130 4.0 12.7 0.6 CZ A:ARG89 4.1 17.1 1.0 NH2 A:ARG89 4.1 12.2 1.0 CB A:LEU129 4.1 12.4 1.0 C A:LEU129 4.2 16.6 1.0 CE2 A:TYR131 4.2 14.0 1.0 CD2 A:TYR131 4.2 14.0 1.0 CA A:LEU129 4.2 13.2 1.0 C A:GLU130 4.2 15.9 0.4 CZ A:TYR131 4.3 16.8 1.0 CG A:TYR131 4.3 12.9 1.0 C A:GLU130 4.3 15.3 0.6 CE1 A:TYR131 4.3 13.5 1.0 CG A:GLU130 4.4 23.8 0.4 CD1 A:TYR131 4.4 13.6 1.0 CA A:TYR131 4.6 11.9 1.0 C A:TYR131 4.6 14.6 1.0 CG A:LEU129 4.6 14.9 1.0 O A:HOH627 4.7 27.1 1.0 CG A:ARG89 4.7 14.9 1.0 O A:HOH912 4.8 29.7 1.0 OH A:TYR131 4.9 16.5 1.0 OE1 A:GLU130 5.0 26.4 0.6

T.Kim, R.Flick, J.Brunzelle, A.Singer, E.Evdokimova, G.Brown, J.C.Joo, G.A.Minasov, W.F.Anderson, R.Mahadevan, A.Savchenko, A.F.Yakunin. Structural and Biochemical Studies of Novel Aldo-Keto Reductases For the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol. Appl. Environ. Microbiol. 2017.
ISSN: ESSN 1098-5336
PubMed: 28130301
DOI: 10.1128/AEM.03172-16