Zinc in PDB 3dfi: The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21

The structure of The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21, PDB code: 3dfi was solved by Y.Zou, J.S.Brunzelle, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	62.940, 62.940, 159.890, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.2

The binding sites of Zinc atom in the The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21 (pdb code 3dfi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21, PDB code: 3dfi:

Zinc binding site 1 out of 1 in the The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Antimicrobial Reagent A40926 Pseudoaglycone Deacetylase DBV21 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:46.0 occ:1.00 OD2 A:ASP19 1.7 50.4 1.0 ND1 A:HIS16 2.2 48.1 1.0 NE2 A:HIS161 2.2 48.4 1.0 O A:HOH356 2.5 41.0 1.0 CG A:ASP19 2.5 51.1 1.0 OD1 A:ASP19 2.6 51.3 1.0 CE1 A:HIS16 3.1 48.0 1.0 CE1 A:HIS161 3.1 48.8 1.0 O A:HOH394 3.2 53.0 1.0 CD2 A:HIS161 3.2 49.1 1.0 CG A:HIS16 3.2 47.7 1.0 CB A:HIS16 3.6 47.9 1.0 CB A:ASP19 4.0 50.3 1.0 NE2 A:HIS16 4.2 48.1 1.0 ND1 A:HIS161 4.3 49.6 1.0 OD1 A:ASP18 4.3 52.7 1.0 CD2 A:HIS16 4.3 46.0 1.0 CG A:HIS161 4.3 47.3 1.0 N A:HIS16 4.4 47.6 1.0 O A:HOH313 4.4 49.9 1.0 CB A:PRO15 4.5 47.3 1.0 CA A:HIS16 4.6 48.4 1.0 OH A:TYR187 4.9 56.4 1.0

Y.Zou, J.S.Brunzelle, S.K.Nair. Crystal Structures of Lipoglycopeptide Antibiotic Deacetylases: Implications For the Biosynthesis of A40926 and Teicoplanin. Chem.Biol. V. 15 533 2008.
ISSN: ISSN 1074-5521
PubMed: 18559264
DOI: 10.1016/J.CHEMBIOL.2008.05.009