Chlorine in PDB 4hzo: The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold

The structure of The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold, PDB code: 4hzo was solved by J.R.Lohman, C.A.Bingman, G.N.Phillips Jr., B.Shen, Enzyme Discovery Fornatural Product Biosynthesis (Natpro), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.39 / 1.76
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	60.487, 60.487, 310.964, 90.00, 90.00, 120.00
R / Rfree (%)	22 / 24.9

The binding sites of Chlorine atom in the The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold (pdb code 4hzo). 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 The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold, PDB code: 4hzo:

Chlorine binding site 1 out of 1 in the The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:35.4 occ:1.00 ND2 A:ASN216 2.9 23.2 1.0 N A:PHE223 3.2 19.5 1.0 CD1 A:TYR222 3.4 18.2 1.0 CD2 A:PHE223 3.5 24.0 1.0 S1P A:COA402 3.7 32.8 1.0 CA A:TYR222 3.7 18.5 1.0 C A:TYR222 3.9 20.6 1.0 CG A:ASN216 3.9 24.1 1.0 C2P A:COA402 4.0 25.6 1.0 CB A:ASN216 4.0 22.2 1.0 CE1 A:TYR222 4.1 25.0 1.0 CB A:PHE223 4.1 20.0 1.0 CA A:PHE223 4.2 20.3 1.0 CG A:PHE223 4.3 22.4 1.0 O A:LEU221 4.4 21.5 1.0 CG A:TYR222 4.4 19.8 1.0 CE2 A:PHE223 4.4 24.4 1.0 CB A:TYR222 4.5 18.1 1.0 N A:TYR222 4.7 20.8 1.0 C A:LEU221 4.9 18.7 1.0

J.R.Lohman, C.A.Bingman, G.N.Phillips, B.Shen. Structure of the Bifunctional Acyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double-Hot-Dog Fold. Biochemistry V. 52 902 2013.
ISSN: ISSN 0006-2960
PubMed: 23320975
DOI: 10.1021/BI301652Y